Abstract
The location, molecular structure, and stage of assembly of viruses and viral components in cells, tissues, and body fluids at various times after infection are important for the understanding of viral diseases. It is equally important to examine in detail the morphological, structural, and molecular alterations occurring in native cell constituents after viral infection.
The submitted manuscript has been authored by a contractor of the U.S. Government under contract No. W-31-109-NG-38. Accordingly the U.S. Government retains a nonexclusive royalty-free license to publish or reproduce the published FORM of this contribution, or allow others to do so, for U.S. Government purposes.
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Keywords
- Sodium Dodecyl Sulfate
- Herpes Simplex Virus Type
- Newcastle Disease Virus
- Vesicular Stomatitis Virus
- Rous Sarcoma Virus
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References
Altevogt P, Fohlman J, Kurnick JT, Peterson P, Wigzell H (1980) Biochemical comparison of HLA-DR molecules derived from autologous human T and B lymphocytes. Eur J Immunol 10: 908–914
Anderson NG (1972) The development of fast analyzers. Z Anal Chem 261: 257–271
Anderson NG, Anderson NL (1978) Analytical techniques for cell fractions. XXI. Two-dimensional analysis of serum and tissue proteins: multiple isoelectric focusing. Anal Biochem 85: 331–340
Anderson NG, Anderson NL (1979) Molecular anatomy. Behring Inst Mitt 63: 169–210
Anderson NG, Anderson NL (1982) The human protein index. Clin Chem 28: 739–748
Anderson NG, Harris WW, Barber AA, Rankin CT Jr, Candler EL (1966) Separation of subcellular components and viruses by combined rate-and isopycnic-zonal centrifugation. Natl Cancer Inst Monogr 21: 253–283
Anderson NG, Waters DA, Nunley CE, Gibson RF, Schilling RM, Denny EC, Cline GB, Babley EF, Peradi TE (1969) K-series centrifuges. I. Development of the K-II continuous-sample-flow-with-banding centrifuge system for vaccine purification. Anal Biochem 32: 460–494
Anderson NG, Willis DD, Holladay DW, Caton JE, Holleman JW, Eveleigh JW, Attrill JE, Ball FL, Anderson NL (1975a) Analytical techniques for cell fractions. XIX. The Cyclum: an automatic system for cyclic chromatography. Anal Biochem 66: 159–174
Anderson NG, Willis DD, Holladay DW, Caton JE, Holleman JW, Eveleigh JW, Attrill JE, Ball FL, Anderson NL (1975b) Analytical techniques for cell fractions. XX. Cyclic affinity chromatography: principles and applications. Anal Biochem 68: 371–393
Anderson NG, Anderson NL, Tollaksen SL (1979a) Proteins of human urine. I. Concentration and analysis of two-dimensional electrophoresis. Clin Chem 25: 1199–1210
Anderson NG, Anderson NL, Tollaksen SL, Hahn H, Giere F, Edwards J (1979b) Analytical techniques for cell fractions. XXV. Concentration and two-dimensional electrophoresis. Anal Biochem 95: 48–61
Anderson NG, Powers MT, Tollaksen SL (1982) Proteins of human milk. I. Identification of major components. Clin Chem 28: 1045–1055
Anderson NL (1981a) High-resolution two-dimensional electrophoretic mapping of immunoglobulin light chains. Immunol Lett 2: 195–199
Anderson NL (1981b) Studies of gene expression in human lymphocytes using high-resolution two-dimensional electrophoresis. In: Allen R, Arnaud P (eds) Electrophoresis ’81. de Gruyter, Berlin, pp 309–316
Anderson NL (1981c) Identification of mitochondrial proteins and some of their precursors in two-dimensional electrophoretic maps of human cells. Proc Natl Acad Sci USA 78: 2407–2411
Anderson NL, Anderson NG (1977) High-resolution two-dimensional electrophoresis of human plasma proteins. Proc Natl Acad Sci USA 74: 5421–5425
Anderson NL, Anderson NG (1978) Analytical techniques for cell fractions. XXII. Two-dimensional analysis of serum and tissue proteins: multiple gradient-slab electrophoresis. Anal Biochem 85: 341–354
Anderson NL, Anderson NG (1979) Microheterogeneity of serum transferrin, haptoglobulin, and a2HS glycoprotein examined by high-resolution two-dimensional electrophoresis. Biochem Biophys Res Commun 88: 258–265
Anderson NL, Hickman BJ (1979) Analytical techniques for cell fractions. XXIV. Isoelectric point standards for two-dimensional electrophoresis. Anal Biochem 93: 312–320
Anderson NL, Taylor J, Scandora AE, Coulter BP, Anderson NG (1981) The TYCHO system for computerized analysis of two-dimensional gel protein mapping data. Clin Chem 27: 1807–1820
Anderson NL, Giometti CS, Gemmell MA, Nance SL, Anderson NG (1982a) A two-dimensional electrophoretic analysis of the heat shock-induced proteins of human cells. Clin Chem 28: 1084–1092
Anderson NL, Nance SL, Pearson TW, Anderson NG (1982) Specific antiserum staining of two- dimensional electrophoretic patterns of human plasma proteins immobilized on nitrocellulose. Electrophoresis 3: 135–142
Bakayev VV, Nedospasov SA (1981) SV-40 specific nucleoprotein complexes: heterogeneity and composition. Virology 109: 244–256
Bachvaroff RJ, Miller F, Rapaport FT (1981) Appearance of cytoskeletal components on the surface of leukemia cells and of lymphocytes transformed by mitogens and Epstein-Barr virus. Proc Natl Acad Sci USA 77: 4979–4983
Beaud G, Dru A (1980) Protein synthesis in vaccinia virus-infected cells in the presence of amino acid analogs: a translational control mechanism. Virology 100: 10–21
Bond CW, Leibowitz JL, Robb JA (1979) Pathogenic murine coronaviruses. II. Characterization of virus-specific proteins of murine coronaviruses JHMV and A-59V. Virology 94: 371–384
Bosselman RA, Price JA, Burns AL, Kaulenas MS, Norkin LC (1978) Ribosomal proteins in normal simian cells, SV-40-transformed simian cells, and simian cells infected with SV-40, adenovirus 5, and vesicular stomatitis virus. Intervirology 9: 8–15
Bossinger J, Miller MJ, Vo KP, Geiduschek EP, Yuong NH (1979) Quantitative analysis of two-dimensional electrophoretograms. J Biol Chem 254: 7986–7998
Brackmann KH, Green M, Wold WSM, Cartas M, Matsuo T, Hashimoto S (1980) Identification and peptide mapping of human adenovirus type 2 induced early polypeptides isolated by two-dimensional gel electrophoresis and immunoprecipitation. J Biol Chem 255: 6772–6779
Bravo R, Celis JE (1980) Gene expression in normal and virally transformed mouse 3T3B and hamster BHK-21 cells. Exp Cell Res 127: 249–260
Brzeski H, Linder S, Krondahl U, Ringertz NR (1980) Pattern of polypeptide synthesis in myoblast hybrids. Exp Cell Res 128: 267–278
Chambers P, Samson ACR (1980) A new structural protein for Newcastle disease virus. J Gen Virol 50: 155–166
Chambers P, Samson ACR (1982) Non-structural proteins in Newcastle disease virus-infected cells. J Gen Virol 58: 1–12
Churchill MA, Radloff RJ (1981) Two-dimensional electrophoretic analysis of encephalomyocarditis viral proteins. J Virol 37: 1103–1106
Cohen GH, Long D, Eisenberg RJ (1980) Synthesis and processing of glycoproteins gD and gC of herpes simplex virus type 1. J Virol 36: 429–439
Deley M, Billiau A, De Somer P (1979) Interferon-induced synthesis of a 63 000 dalton protein in mouse cells. Biochem Biophys Res Commun 89: 701–705
Dubovi EJ, Wagner RR (1977) Spatial relationships of the proteins of vesicular stomatitis virus induction of reversible oligomers by cleavable protein cross-linkers and oxidation. J Virol 22: 500–509
Eaton BT (1982) Transient enhanced synthesis of a cellular protein following infection of aedes albopictus cells with sindbis virus. Virology 117: 307–321
Edwards JJ, Anderson NG (1981) The nature of observed schlieren patterns in isoelectric focusing gels and their use for position location of banded proteins. Electrophoresis 2: 161–168
Edwards JJ, Anderson NG, Nance SL, Anderson NL (1979) Red-cell proteins. I. Two-dimensional mapping of human erythrocyte lysate proteins. Blood 53: 1121–1132
Edwards J J, Tollaksen SL, Anderson NG (1981) Proteins of human semen. I. Two-dimensional mapping of human seminal fluid. Clin Chem 27: 1335–1340
Edwards J J, Tollaksen SL, Anderson NG (1982) Proteins of human urine. III. Identification and two-dimensional electrophoretic map positions of some major urinary proteins. Clin Chem 28: 941–948
Elliott RM, Bravo R, Kelly DC (1980) Frog virus 3 replication: analysis of structural and nonstructural polypeptides in infected BHK cells by acidic and basic two-dimensional gel electrophoresis. J Virol 33: 18–27
Esche H (1982) Viral gene products in adenovirus type-2 transformed hamster cells. J Virol 41: 1076–1082
Esche H, Siegman B (1982) Expression of early viral gene products in adenovirus type 12-infected and -transformed cells. J Gen Virol 60: 99–113
Faissner A, Darai G, Flugel RM (1980) Identification of polypeptides of the three shrew (Tupaia) adenovirus. Intervirology 14: 272–276
Faissner A, Darai G, Flugel RM (1982) Analysis of polypeptides of the three shrew (Tupaia) herpes virus by gel electrophoresis. J Gen Virol 58: 139–148
Fanning E, Burger C, Gurney EG (1981) Comparison of T antigen-associated host phosphoproteins from SV-40-infected and SV-40-transformed cells of different species. J Gen Virol 55: 367–378
Forchhammer J, Turnock G (1978) Glycoproteins from murine C-type virus are more acidic in virus derived from transformed cells than from nontransformed cells. Virology 88: 177–182
Fox RI, Weissman IL (1979) Moloney virus-induced cell surface antigens and histocompatibility antigens are located on distinct molecules. J Immunol 122: 1697–1704
Garrels JI (1979) Two-dimensional gel electrophoresis and computer analysis of proteins synthesized by clonal cell lines. J Biol Chem 254: 7961–7977
Gemmell MA, Anderson NL (1982) Lymphocyte, monocyte, and granulocyte proteins compared by use of two-dimensional electrophoresis. Clin Chem 28: 1062–1066
Gilmore TD, Radke K, Martin GS (1982) Tyrosine phosphorylation of a 50-kilodalton cellular polypeptide associated with the rous sarcoma virus transforming protein PP-60 S-R-C. Mol Cell Biol 2: 199–206
Giometti CS, Anderson NG (1979) Two-dimensional electrophoresis of human saliva. In: Radola B (ed) Electrophoresis ’79. de Gruyter Berlin, pp 395–404
Giometti CS, Anderson NL (1981a) A variant of human nonmuscle tropomyosin found in fibroblasts by using two-dimensional electrophoresis. J Biol Chem 256: 11840–11846
Giometti CS, Anderson NG (1981b) Muscle protein analysis. III. Analysis of frozen tissue sections using two-dimensional electrophoresis. Clin Chem 27: 1918–1921
Giometti CS, Anderson NG, Anderson NL (1979) Muscle protein analysis. I. Development of high-resolution two-dimensional electrophoresis of skeletal muscle proteins for analysis of microbiopsy samples. Clin Chem 25: 1877–1884
Giometti CS, Barany M, Danon MJ, Anderson NG (1980a) Muscle protein analysis. II. Two-dimensional electrophoresis of normal and diseased human skeletal muscle. Clin Chem 26: 1152–1155
Giometti CS, Anderson NG, Tollakson SL, Edwards JJ, Anderson NL (1980b) Analytical techniques for cell fractions. XXVII. Use of heart proteins as reference standards in two-dimensional electrophoresis. Anal Biochem 102: 47–58
Giometti CS, Willard KE, Anderson NL (1982) Cytoskeletal proteins from human skin fibroblasts, peripheral blood leukocytes, and a lymphoblastoid cell line compared by two-dimensional gel electrophoresis. Clin Chem 28: 955–961
Griffiths PD, Buie KJ, Heath RB (1980) Persistence of high-titre antibodies to the early antigens of cytomegalovirus in pregnant women. Arch Virol 64: 303–309
Haarr L, Marsden HS (1981) Two-dimensional gel analysis of herpes simplex virus type 1-induced polypeptides and glycoprotein processing. J Gen Virol 52: 77–92
Hamann A, Wiegers KJ, Drzeniek R (1977) Isoelectricfocusing and two-dimensional analysis of poliovirus proteins. Virology 78: 359–362
Harris WW, Anderson NG, Bartlett TW, Rutenberg EL, McCauley LL, Kniseley RM (1966) Unusual particles in human plasma from leukemia and lymphosarcoma. Natl Cancer Inst Monogr 21: 389–396
Heilman CR Jr, Zweig M, Hampar B (1981) Herpes simplex virus type 1 and 2 intracellular P-40 type specific and cross-reactive antigenic determinants on peptides generated by partial proteolysis. J Virol 40: 508–515
Hendricks M, Weintraub H (1981) Tropomyosin is decreased in transformed cells. Proc Natl Acad Sci USA 78: 5633–5637
Horisberger MA (1980) The large P proteins of influenza A viruses are composed of 1 acidic and 2 basic polypeptides. Virology 107: 302–305
Hsu C-H, Kingsbury DW (1982) NS phosphoprotein of vesicular stomatitis virus: subspecies separated by electrophoresis and isoelectric focusing. J Virol 42: 342–345
Ichihashi Y (1981) Unit complex of vaccinia polypeptides linked by disulfide bridges. Virology 113: 277–284
Isaka T, Ikawa Y, Yoshida M (1978) Characterization of transformation-sensitive membrane proteins in chick embryo fibroblasts transformed with avian sarcoma virus. Virology 90: 330–343
Jaye M, Wu F-S, Lucas-Lenard JM (1980) Inhibition of synthesis of ribosomal proteins and of ribosome assembly after infection of L cells with vesicular stomatitis virus. Biochim Biophys Acta 606: 1–12
Kamine J, Burr JG, Burr ME, Buchanan JM (1977) 2-Dimensional electrophoresis of proteins synthesized in vitro from RNA of Rous sarcoma virus. J Cell Biol 75: 395A
Karshin WL, Arcement LJ, Naso RB, Arlinghaus RB (1977) Common precursor for Rauscher leukemia virus gp 69–71, pl5(E) and pl2(E). J Virol 23: 787–798
Kilpatrick D, Rouhandeh H (1981) The polypeptides of monkey poxvirus. I. Analysis of the polypeptide synthesis of monkey poxvirus by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by 2-dimensional electrophoresis. Virology 110: 455–465
Kingsford L, Emerson SU, Kelley JM (1980) Separation of cyanogen bromide-cleaved peptides of the vesicular stomatitis virus glycoprotein and analysis of their carbohydrate content. J Virol 36: 309–316
Kobayashi N, Tanaka A, Kaji A (1981) In vitro phosphorylation of the 36K protein in extract from Rous sarcoma virus-transformed fibroblast. J Biol Chem 256: 3053–3058
Laszlo A, Radke K, Chin S, Bissell MJ (1981) Tumor promoters alter gene expression and protein phosphorylation in avian cells in culture. Proc Natl Acad Sci USA 78: 6241–6245
Leavitt JC, Phelan MA, Leavitt AH, Mayner RE, Ennis FA (1979) Human influenza A virus. Comparative analysis of the structural polypeptides by 2-dimensional polyacrylamide gel electrophoresis. Virology 99: 340–348
Ledbetter JA (1979) Two-dimensional analysis of murine leukemia virus gaggene polyproteins. Virology 95: 85–98
Lemkin P, Merril C, Lipkin L, Vankeuren M, Oertel W, Shapiro B, Wade M, Schultz M, Smith F (1979) Software aids for the analysis of two-dimensional gel electrophoresis images. Comput Biomed Res 12: 517–544
Maack CA, Penhoet EE (1980) Biochemical characterization of the TSE-1 mutant of vesicular stomatitis virus: New-Jersey serotype alterations in the NS protein. J Biol Chem 255: 9249–9254
Mariash CN, Seeling S, Oppenheimer JH (1982) A rapid, inexpensive, quantitative technique for the analysis of two-dimensional electrophoresis. Anal Biochem 121: 388–394
Marvaldi J, Lucas-Lenard J (1977) Differences in the ribosomal protein gel profile after infection of L cells with wild type or temperature sensitive mutants of vesicular stomatitis virus. Biochemistry 16: 4320–4327
McCahon D (1981) The genetics of aphthovirus. Arch Virol 69: 1–23
McConkey EH (1982) Molecular evolution, intracellular organization, and the quinary structure of proteins. Proc Natl Acad Sci USA 79: 3236–3240
Meruelo D, Nimelstein SH, Jones PP, Liebermann M, McDevitt HO (1978) Increased synthesis and expression of H-2 antigens on thymocytes as a result of radiation leukemia virus infection. A possible mechanism for H-2-linked control of virus-induced neoplasia. J Exp Med 147: 470–487
Milavetz BI, Spotila LD, Thomas R, Huberman JA (1980) Two-dimensional analysis of proteins sedimenting with SV-40 chromosomes. J Virol 35: 854–864
Mudds J A, Swanson RE (1978) In situ cross-linking of vesicular stomatitis virus proteins with reversible agents. Virology 88: 263–280
Nagai Y, Yoshida T, Hamaguchi M, Iinuma M, Maeno K, Matsumoto T (1978) Cross-linking of Newcastle disease virus proteins. Arch Virol 58: 15–28
Naito S, Matsumoto S (1978) Identification of cellular actin within the Rabies virus. Virology 91: 151–163
Nance SL, Hickman BJ, Anderson NL (1980) A method for studying proteins in 2-D gels using thermal denaturation analysis. In: Radola B (ed) Electrophoresis ’79. de Gruyter, Berlin, pp 351–360
Nusse R, Janssen H, de Vries L, Michalides R (1980) Analysis of secondary modifications of mouse mammary tumor virus proteins by 2- dimensional gel electrophoresis. J Virol 35:340– 348
O’Farrell PH (1975) High-resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007–4021
Petri T, Dimmock NJ (1981) Phosphorylation of influenza virus nucleoprotein in vivo. J Gen Virol 57: 185–190
Ponder BAJ, Robbins AK, Crawford LV (1977) Phosphorylation of polyoma and SV-40 virus proteins. J Gen Virol 37: 75–83
Privalsky ML, Penhoet EE (1978) Influenza virus proteins: identity, synthesis, and modification analyzed by two-dimensional gel electrophoresis. Proc Natl Acad Sci USA 75: 3625–3629
Racevskis J, Sarkar NH (1980) Murine mammary tumor virus structural protein interactions: formation of oligomeric complexes with cleavable cross-linking agents. J Virol 35: 937–948
Radke K, Martin GS (1979) Transformation by Rous sarcoma virus: effects of SRC gene expression on the synthesis and phosphorylation of cellular polypeptides. Proc Natl Acad Sci USA 76: 5212–5216
Radke K, Gilmore T, Martin GS (1980) Transformation by Rous sarcoma virus: a cellular substrate for transformation-specific protein phosphorylation contains phosphotyrosine. Cell 21: 821–828
Reeves R, Cserjesi P (1979) Constitutive synthesis of globins within most of the members of an uninduced proliferating population of Friend erythroleukemic cells. Dev Biol 69: 576–588
Richardson CD, Vance DE (1978) Chemical cross-linking of proteins of Semliki-forest virus. Virus particles and plasma membranes from BHK-21 cells treated with colchicine or dibucaine. J Virol 28: 193–198
Roubal J, Kallin B, Luka J, Klein G (1981) Early DNA-binding polypeptides of Epstein-Barr virus. Virology 113: 285–292
Samson ACR, Chambers P, Dickinson JH (1980) Location of post-translational cleavage events within F and HN glycoproteins of Newcastle disease virus. J Gen Virol 47: 19–27
Samson ACR, Chambers P, Lee CM, Simon E (1981) Temperature-sensitive mutant of Newcastle disease virus which has an altered nucleocapsid-associated protein. J Gen Virol 54: 197–202
Scheele GA (1975) Two-dimensional gel analysis of soluble proteins. Characterization of guinea pig exocrine pancreatic proteins. J Biol Chem 250: 5375–5385
Schneider J, Falk H, Hunsmann G (1980) Envelope polypeptides of Friend leukemia virus: purification and structural analysis. J Virol 33: 597–605
Shiu RPC, Pastan IH (1979) Properties and purification of a glucose-regulated protein from chick embryo fibroblasts. Biochim Biophys Acta 576: 141–150
Smith GW, Hightower LR (1981) Identification of the P proteins and other disulfide-linked and phosphorylated proteins of Newcastle disease virus. J Virol 37: 256–267
Strand M, August JT (1977) Polypeptides of cells transformed by RNA or DNA tumor viruses. Proc Natl Acad Sci USA 74: 2729–2733
Strand M, August JT (1978) Polypeptide maps of cells infected with murine type C leukemia or sarcoma oncovirus. Cell 13: 399–408
Symington J, Green M, Brackmann K (1981) Immunoautoradiographic detection of proteins after electrophoretic transfer from gels to diazo-paper: analysis of adenovirus-encoded proteins. Proc Natl Acad Sci USA 78: 177–181
Takemoto LJ, Fox CF, Jensen FC, Elder JH, Lerner RA (1978) Nearest neighbor interactions of the major RNA tumor virus glycoprotein on murine cell surfaces. Proc Natl Acad Sci USA 75: 3644–3648
Taylor J, Anderson NL, Coulter BP, Scandora AE, Anderson NG (1980) Estimation of two-dimensional electrophoretic spot intensities and positions by modeling. In: Radola B (ed) Electrophoresis ’79. de Gruyter, Berlin, pp 329–339
Taylor J, Anderson NL, Anderson NG (1981) A computerized system for matching and stretching two-dimensional gel patterns represented by parameter lists. In: Allen RC, Arnaud P (eds) Electrophoresis ’81. de Gruyter, Berlin, pp 383–400
Taylor J, Anderson NL, Scandora AE Jr, Willard KE, Anderson NG (1982) Design and implementation of a prototype human protein index. Clin Chem 28: 861–866
Thimmig RY, Hughes JV, Kinders RJ, Milenkovic AG, Johnson TC (1980) Isolation of glycoprotein of vesicular stomatitis virus and its binding to cell surfaces. J Gen Virol 50: 279–292
Tollaksen SL, Anderson NG (1980) Two-dimensional electrophoresis of human urinary proteins in health and disease. In: Radola B (ed) Electrophoresis ’79. de Gruyter, Berlin, pp 405–414
Tollaksen SL, Edwards JJ, Anderson NG (1981) The use of carbamylated charge standards for testing batches of ampholytes used in two-dimensional electrophoresis. Electrophoresis 2: 155–160
Tschannen R, Schafer R (1980) Strain and host cell dependence of vaccinia virus proteins. Eur J Biochem 111: 145–150
Tuszynski GP, Frank ED, Damsky CH, Buck CA, Warren L (1979) The detection of smooth muscle Desmin-like protein in BHK21 /C13 fibroblasts. J Biol Chem 254: 6138–6143
Ulmanen I, Broni BA, Krug RM (1981) Role of 2 the influenza virus core P proteins in recognizing Cap 1 structures of RNA and in initiating viral RNA transcription. Proc Natl Acad Sci USA 78: 7355–7359
Vafai A, Rouhandeh H (1981) Yaba virus polypeptides. 3. Analysis of virus-induced polypeptides in infected cells by two-dimensional gel electrophoresis (Abstr). Annu Meet Am Soc Microbiol 81: 231
Van Dyke TA, Flanegan JB (1980) Identification of poliovirus polypeptide P-63 as a soluble RNA- dependent RNA polymerase. J Virol 35: 732–740
Weil J, Espstein LB, Epstein CJ (1980) Synthesis of interferon-induced polypeptides in normal and chromosome 21 aneuploid human fibroblasts: relationship to relative sensitivities in antiviral assays. J Interferon Res 1: 111–124
Wiegers KJ, Dernick R (1981) Polio virus-specific polypeptides in infected Hela cells analyzed by isoelectric focusing and 2-D analysis. J Gen Virol 52: 61–69
Willard KE (1982a) Two-dimensional analysis of human lymphocyte proteins. II. Regulation of lymphocyte proteins by a molecule present in normal human urine. Clin Chem 28: 1074–1083
Willard KE (1982b) Two-dimensional analysis of human lymphocyte proteins. III. Preliminary report on a marker for the early detection and diagnosis of infectious mononucleosis. Clin Chem 28: 1031–1035
Willard KE, Anderson NL (1980) Alterations of two-dimensional electrophoretic maps of human peripheral blood lymphocytes induced by concanavalin A. In: Radola B (ed) Electrophoresis ’79. de Gruyter, Berlin, pp 415–424
Willard KE, Anderson NG (1981) Two-dimensional analysis of human lymphocyte proteins. I. An assay for lymphocyte effectors. Clin Chem 27: 1327–1334
Willard KE, Giometti CS, Anderson NL, O’Connor TE, Anderson NG (1979) Analytical techniques for cell fractions. XXVI. Two-dimensional electrophoretic analysis of basic proteins using phosphatidyl choline urea solubilization. Anal Biochem 100: 289–298
Willard KE, Thorsrud AK, Munthe E, Jellum E (1982) Two-dimensional electrophoretic analysis of human leukocyte proteins from patients with rheumatoid arthritis. Clin Chem 28: 1067–1073
Yoshikura H, Tejima S, Kuchino T, Segawa K, Odaka T (1982) Characterization of N-type and dually permissive cells segregated from mouse fibroblasts whose Fv-1 phenotype could be modified by another independently segregating gene(s). J Virol 41: 145–152
Yuasa Y, Hirai R, Huh N, Segawa K (1980) Double transformation of Indian muntjac muntiacus-muntjac cells by Avian sarcoma virus and murine sarcoma virus. Jap J Exp Med 50: 23–34
Zarling DA, Watson A, Bach FH (1980) Mapping of lymphocyte surface polypeptide antigens by chemical cross-linking with bis-2 succinimidooxycarbonyloxyethyl sulfone. J Immunol 124: 913–920
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Anderson, N.G. (1983). High-Resolution Protein Separation and Identification Methods Applicable to Virology. In: Bachmann, P.A. (eds) New Developments in Diagnostic Virology. Current Topics in Microbiology and Immunology, vol 104. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-68949-9_12
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