Proteinase inhibitors from Vigna unguiculata subsp. cylindrica: III. Properties and kinetics of inhibitors of papain, subtilisin, and trypsin

Comparative data on the properties of four thiol proteinase inhibitors, and of four serine proteinase inhibitors (two subtilisin and two trypsin inhibitors) isolated from seeds of Vigna are presented. They were similar in their molecular weights (5000–15,000) and dissociation constants (10 −8–10 −9...

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Veröffentlicht in:	Archives of biochemistry and biophysics 1980, Vol.204 (1), p.134-140
Hauptverfasser:	Vartak, H.G., Rele, Meenakshi V., Jagannathan, V.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - analysis Chemical Phenomena Chemistry Kinetics Molecular Weight Papain - antagonists & inhibitors Protease Inhibitors - isolation & purification Protease Inhibitors - pharmacology Protein Binding Seeds - analysis Subtilisins - antagonists & inhibitors Trypsin Inhibitors - isolation & purification Trypsin Inhibitors - pharmacology
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