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Identification and Characterization of Brush Border Membrane Bound Carboxypeptidase P from Rat Small Intestine
쥐 소장점막의 Carboxypeptidase P

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Authors
Song, In Sung
Issue Date
1985-09
Publisher
Seoul National University College of Medicine
Citation
Seoul J Med, Vol.26 No.2, pp. 213-219
Keywords
Carboxypeptidase PRat small intestineBrush border membrane
Abstract
Carboxypeptidase P in rat small intestine was identified and characterized using
N-CBZ-Gly-Pro-Leu and N-CBZ-Pro-Ala as substrates, of which the hydrolysis was monitored
by amino acid analyzer.
Specific carboxypeptidase P activites in bursh border membranes were increased 8 fold over
that in the mucosal homogenate, Carboxypeptidase P had a pH optimum, 7,5 and activities
were totally disappeared after incubation at 60°C for 20 min, Carboxypeptidase P activities
were strongly inhibited by metalloenzyme inhibitors and reactivated by addition of Co'; to
EDTA-treated brush border membranes, Molecular weight of carboxypeptidase was 259,000,
Regional and cellular distribution of carboxypeptidase P suggested a physiologic role of this
enzyme in protein digestion. ;
단백분해효소인 carboxypeptidase P의 존재를 쥐 소장점막 미소 융모막에서 확인하고 그 효소적 특징을 조사하였다.
효소활성도는 N-CBZ-Gly-Pro-Leu와 N-CBZ-Pro-Ala를 기질로 하여, 분해산물은 단백산 분석기를 이용, 측정하였다.
Carboxypeptidase P 활성도는 점막균등액에 비해 미소융모막에 8배 증가되어 있었고, 효의 적정 pH는 7.5이었으며, 60℃에서 20분간 전처치로 효소활성도가 없어짐을 알 수 있었다.
효소활성도는 금속효소 억제인자에 의해 강력히 억제되었으며, 억제물질인 EDTA로 전처치된 미소 융모막에 Co++의 첨가로 효소가 재활성화되었다.
전기영동법에 의해 측정된 carboxypeptidase P의 분자량은 259,000이었다.
효소의 소장에서의 지역적 분포나 세포내 분포상태는 단백분해흡수에 있어서 carboxypeptidase P의 생리적 기능을 시사하고 있었다.
ISSN
0582-6802
Language
English
URI
https://hdl.handle.net/10371/6163
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Medicine (의학과)The Seoul Journal of MedicineThe Seoul Journal of Medicine Vol. 26 No.2 (1985)
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