[Characteristics of the kallikreins in healthy and malignant (adenocarcinoma) mucous membrane of the human large intestine].
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.
D000230:Adenocarcinoma / Q000201:enzymology*; D007611:Aprotinin / Q000378:metabolism; D006801:Humans; D007413:Intestinal Mucosa / Q000201:enzymology*; D007414:Intestinal Neoplasms / Q000201:enzymology*; D007420:Intestine, Large / Q000201:enzymology*; D007610:Kallikreins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007705:Kinins / Q000378:metabolism; D014357:Trypsin / Q000494:pharmacology
D007705:Kinins; D007611:Aprotinin; D007610:Kallikreins; D014357:Trypsin
Kharakteristika kallikreinov zdorovoĭ i malignizirovannoĭ (adenokartsinoma) slizistoĭ obolochki tolstoĭ kishki cheloveka.