Procathepsins L and D are membrane-bound in acidic microsomal vesicles
نویسندگان
چکیده
منابع مشابه
Selective Release of Content from Microsomal Vesicles without Membrane Disassembly
Rough and smooth microsomes were shown to have similar sets of polypeptide chains except for the proteins of ribosomes bound to the rough endoplasmic reticulum (ER). More than 50 species of polypeptides were detected by acrylamide gel electrophoresis, ranging in molecular weight from 10,000 to approximately 200,000 daltons. The content of rough and smooth microsomes was separated from the membr...
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Two lysosomal proenzymes, procathepsins L and D, bind to mouse fibroblast microsomal membranes at acidic pH. This membrane association is independent of the mannose-6-phosphate receptors and requires the presence of the N-terminal propeptides of the enzymes. We have identified the protein that specifically binds procathepsin L at pH 5. A 43-kDa membrane protein coimmunoprecipitated with procath...
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Supplementary Material Available: Preparative methods for the starting materials, stereochemical assignments of 1,3-diols listed in Table I, and 400-M Hz 'H N M R spectra of acetonides of 1-3 and 7 (6 pages). Ordering information is given on any current masthead page. The Cytochrome P-450 dependent monooxygenases are mem brane-bound enzymes that catalyze a great variety of reactions, among whi...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)98635-7