Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Extracts of mammalian arterial walls revealed a kinin-like biological activity resistant against proteolytic inactivation with trypsin but not chymotrypsin. Bradykinin was chromatographically determined as kinin existing in extracts from the rat aorta. Kallidin was found as well as bradykinin in human vessels. Metabolism of vasoactive kinins in the vascular wall seems to take part in control of circulation and blood pressure.
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PMID:[Possible participation of vessel wall kinins in regulating blood vessel tonus]. 342 24

Partially purified kinin, a polypeptide in wasp venom, has been found to be a potent smooth-muscle stimulating and hypotensive agent. Such a preparation was 10 to 100 times more effective than histamine in enhancing capillary permeability on intradermal injection, and 10 times more effective than acetylcholine in evoking pain on a cutaneous blister base. Some differences between the actions of salivary kallikrein and trypsin in releasing kallidin or bradykinin have been observed, and some modifications of previous methods of preparing crude kallidin and bradykinin are suggested. Kallidin and bradykinin are effective enhancers of capillary permeability in the guinea-pig and rabbit. Chemical and pharmacological tests failed to differentiate between kallidin and bradykinin which must be, therefore, closely similar compounds. The possible role of kallidin and bradykinin in physiological or pathological conditions is discussed.
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PMID:A comparative study of kinin, kallidin, and bradykinin. 1344 66

The plasma globulins which produce the vasoactive polypeptides, bradykinin, kallidin and angiotensin, have been compared. After incubation of plasma with kallikrein and exhaustion of its kallidinogen, subsequent incubation with trypsin did not result in formation of bradykinin, showing that bradykininogen had also been exhausted and suggesting that kallikrein and trypsin use the same substrate. Kallidin and bradykinin formation was not prevented by acid-treatment of plasma, though heat-denatured substrate produced kallidin less readily. Kallikrein could exhaust plasma bradykininogen without affecting levels of angiotensinogen. Following nephrectomy of dogs, plasma angiotensinogen levels rose whereas bradykininogen levels did not. These results confirm the belief that bradykininogen differs from angiotensinogen but not from kallidinogen.
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PMID:BRADYKININOGEN, ANGIOTENSINOGEN AND KALLIDINOGEN. 1408 56