Degradation of Ra-reactive Factor by Proteases in Cells of Promonocytic Line, U937
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概要
- 論文の詳細を見る
To investigate the fate of polypeptides of Ra-reactive factor (RaRF) in phagocytic cells, the RaRF was incubated with lysosomal fractions of human monocytic cell line U937. A 30-kDa fragment generated when the RaRF was incubated with the extract from heavy lysosomal (P1) fraction. Immunoblot analysis demonstrated that this fragment was produced from the 35-kDa polysaccharide binding component of RaRF by cleavage with an enzyme in the lysosomal extract. This reaction was not inhibited by EDTA. Elastase is a candidate of this enzyme because elastase of polymorphonuclear leucocytes produced a 30 kDa band, but trypsin, cathepsin G and Cls did not.
- 北里大学の論文
- 1994-12-31
著者
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Ji Y‐h
Kitasato Univ. School Of Medicine
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Hatsuse Hiromi
Department of Molecular Biology, School of Medicine, Kitasato University.
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Kawakami Masaya
Department of Molecular Biology, School of Medicine, Kitasato University.
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Zhou Hong
Department of Social Medicine & Health Education, School of Public Health, Peking University
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Zhou Hong
Department Of Microbiology The Tianjin Medical College
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Zhou Hong
Department Of Chemistry Of Natural Drugs School Of Pharmacy Fudan University
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Hatsuse Hiromi
Department Of Molecular Biology Kitasato University School Of Medicine
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Ji Yu-Hua
Department of Molecular Biology, Kitasato University School of Medicine
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Zhou H
Fudan Univ. Shanghai Chn
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Zhou Hong
Department Of Anatomy And Molecular Histology Interdisciplinary Graduate School Of Medicine And Engi
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Kawakami Masaya
Department Of Molecular Biology Kitasato University School Of Medicine
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