VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Characteristics of the kallikreins in healthy and malignant (adenocarcinoma) mucous membrane of the human large intestine

   
Paskhina T.S., Nartikova V.F., Egorova T.P., Gorbeshko T.P.
PubMed Id: 6201001
Year: 1984  Volume: 30  Issue: 1  Pages: 87-96
Total kininogenase activity was higher by 50% in supernatant of malignant mucosa homogenate as compared with normal tissue. But specific kininogenase and N-acetyl-arginine esterase activity were distinctly similar both in normal and tumoral tissues; N-ac-arg esterase activity tended to decrease in malignant mucosa. Partially purified preparations of kallikrein, isolated from adenocarcinoma and normal mucosa of human large intestine, were distinctly identical in their properties: both these enzymes were not inhibited by soybean trypsin inhibitor, they were highly sensitive to main pancreatic inhibitor from bovine tissues (Ki = 10(-10) M) and their molecular mass was about 40,000 daltons. The data obtained suggest that these enzymes may be concerned with tissue kallikreins. Highly purified preparation of kininogenase (85-90% of purity) first obtained from adenocarcinoma of human ascending colon, was identify with tissue kallikreins as it hydrolyzed low molecular kininogen, liberating the kinin--lysyl-bradykinin.
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Paskhina T.S., Nartikova V.F., Egorova T.P., Gorbeshko T.P. (1984) Voprosy meditsinskoi khimii, 30(1), 87-96.
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