Abstract
Our studies on the amino acid sequence of pig pancreatic kallikrein B (EC 3.4.21.8) have been performed with a preparation (1) that had been treated with neuraminidase to remove bound sialic acids. After reductive cleavage of the disulfide bridges and carboxymethylation, two peaks of UV-absorbing material could be separated by gel filtration on Sephadex G-75 in 50% acetic acid. According to gel electrophoresis, both were essentially homogeneous. Evidently, pig pancreatic kallikrein is composed of two chains presumably held together by disulfide bridges, as it had already been inferred from the presence of two amino terminal and two C-terminal amino acid residues (2).
This work has been supported by the Deutsche Forschungsgemeinschaft, Bonn-Bad Godesberg, the Sonderforschungsbereich 51, München, and the Stiftung Volkswagenwerk, Hannover.
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Tschesche, H. et al. (1976). The Primary Structure of Pig Pancreatic Kallikrein B. In: Sicuteri, F., Back, N., Haberland, G.L. (eds) Kinins. Advances in Experimental Medicine and Biology, vol 70. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3267-1_17
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