This chapter reproduces in modified form a contribution on Golgi apparatus biochemistry prepared for the centennial year of Golgi apparatus discovery by Thomas W. Keenan (Keenan, 1998). The chapter contents overlap topics of other chapters in the book but many are given in greater detail and from a different prospective such that the sense of the original text and references has been retained.

Biochemical studies of the Golgi apparatus were possible only when isolated fractions in useful yield and fraction purity were developed in the late 1960s and early 1970s first from plants (Morré and Mollenhauer, 1964) and rat liver (Morré et al., 1969, 1970a) and later from other tissues and eventually from cultured cells. Detailed methodology is provided in Chapter 3. Early studies focused on marker enzymes as a means of assessing fraction purity and enrichment and glycosyltransferases, the latter already inferred from an abundant literature reporting cytochemical and electron microscope—autoradiographic studies that revealed the Golgi apparatus to be a site of protein glycosylation (Peterson and LeBlond, 1964).


Golgi Apparatus Early Endosome Copper Ferrocyanide Golgi Appa Sugar Nucleotide Donor 


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© Springer-Verlag Berlin Heidelberg 2009

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