PMID: 6988008Mar 14, 1980Paper

Multiple forms of the asclepains. Cysteinyl proteases from milkweed

Biochimica Et Biophysica Acta
K R LynnN A Clevette

Abstract

Two groups of asclepains (EC 3.4.22.7) isolated from the latex of Asclepias syriaca L. (milkweed) were each separated into five homogeneous enzymes. The members of each group are of similar amino acid composition, and leucine is the common N-terminal residue. Michaelis values are reported for each of the component cysteinyl proteases of milkweek latex, and are compared with those of analogous enzymes from other plant sources. The asclepains all catalysed the hydrolysis of insulin B chain to yield similar two-dimensional maps. The peptides produced from one such digestion were characterized and scission points were defined and compared with those for papain.

References

Aug 15, 1979·Biochimica Et Biophysica Acta·K R Lynn
Jan 1, 1977·Analytical Biochemistry·K R Lynn
Apr 1, 1975·Archives of Biochemistry and Biophysics·R M Silverstein, F J Kezdy
Feb 12, 1970·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·A Berger, I Schechter
Nov 1, 1972·FEBS Letters·M J Boland, M J Hardman
Nov 1, 1969·Plant Physiology·D E Kramer, J R Whitaker

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Citations

Feb 8, 2016·Applied Biochemistry and Biotechnology·Cynthia SequeirosSebastián A Trejo
Sep 6, 2011·Biotechnology Advances·Nuria González-RábadeMaría Del Carmen Oliver-Salvador
Feb 26, 2008·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Chi-Min Kao, Fore-Lien Huang
Jul 1, 1984·Archives of Biochemistry and Biophysics·A SenguptaN K Sinha
Feb 11, 2009·Acta Biochimica Et Biophysica Sinica·Constanza LiggieriNora Priolo
Feb 23, 1995·Biochimica Et Biophysica Acta·K OhtsukiM Kawabata
Aug 21, 1980·Biochimica Et Biophysica Acta·K R LynnC Roy

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