کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10820574 1060718 2005 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Partial purification and characterization of pro-phospholipase A2 activating proteases from gill membranes of the red sea bream, Chrysophrys major
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Partial purification and characterization of pro-phospholipase A2 activating proteases from gill membranes of the red sea bream, Chrysophrys major
چکیده انگلیسی
We previously reported that gill group IB secretory phospholipase A2 (sPLA2) exists as an inactive pro-sPLA2 with the dipeptide Ala-Arg, at the N-terminus of mature sPLA2 in mucous cells. Pro-sPLA2 should be activated after being secreted to the surface of gill epithelia by trypsin-like protease. To clarify the above hypothesis, we investigated the existence of pro-sPLA2 activating protease (PAP) in the gills of the red sea bream, using gill pro-sPLA2 as a substrate. PAP was solubilized from the membrane fraction of the gills with 2% sodium cholate and partially purified by benzamidine-Sepharose chromatography and reversed-phase HPLC. Partially purified proteases, PAP1 and PAP2 showed a high molecular mass of about 200 kDa by gelatin zymography. PAP1 and PAP2 had optimal pH from 7 to 9 and were inhibited by trypsin inhibitors. These properties of PAP1 and PAP2 suggest that both enzymes belong to the membrane-associated trypsin-like serine protease family, such as enteropeptidase and corin. This is the first report verifying the existence of the activating protease of group IB pro-sPLA2 isoforms in a non-digestive tissue.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 141, Issue 1, May 2005, Pages 121-127
نویسندگان
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