Effect of blood plasma inhibitors on activity of serine and cysteine proteinases

Data on study of action plasma inhibitors on activity of pancreatic proteolytic enzymes (trypsin, chymotrypsin) and plant proteinases (papain, bromelain), included in composition of enzyme mixes, used for orally application are submitted. It is established, that serine proteases are more sensitive t...

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Bibliographic Details
Published in:	Ukrainskij biohimičeskij žurnal Vol. 70; no. 6; p. 35
Main Authors:	Veremeenko, K N, Kizim, A I, Terzov, A I, Dosenko, V E, Nosenko, O A
Format:	Journal Article
Language:	Russian
Published:	Ukraine 01-11-1998
Subjects:	Animals Caseins - metabolism Cysteine Endopeptidases - metabolism Cysteine Endopeptidases - pharmacokinetics Cysteine Proteinase Inhibitors - blood Cysteine Proteinase Inhibitors - pharmacology Humans Hydrolysis Serine Endopeptidases - metabolism Serine Endopeptidases - pharmacokinetics Serine Proteinase Inhibitors - blood Serine Proteinase Inhibitors - pharmacology
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Summary:	Data on study of action plasma inhibitors on activity of pancreatic proteolytic enzymes (trypsin, chymotrypsin) and plant proteinases (papain, bromelain), included in composition of enzyme mixes, used for orally application are submitted. It is established, that serine proteases are more sensitive to inactivation of plasma inhibitors, than cysteine enzymes. Main inhibitor of the papain and bromelain is alpha-2-macroglobulin in complex with which they preserve significant part of initial activity. A high-sensitivity method of determination of activity enzyme combinations, enabling to detect nanograms of them in presence of plasma inhibitors is offered. It can be used for study pharmacokinetic and optimization of enzyme mixes application in clinical practice.
ISSN:	0201-8470