| Purificaton and characterization of a pepsinogen and its pepsin from proventriculus of the Japanese quail. | |
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MedLine Citation:
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PMID: 6766746 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A crude extract of the proventriculus of the Japanese quail gave at least five bands of peptic activity at pH 2.2 on polyacrylamide gel electrophoresis. The main component, constituting about 40% of the total acid protease activity, was purified to homogeneity by hydroxyapatite and DEAE-Sepharose column chromatographies. At below pH 4.0, the pepsinogen was converted to a pepsin, which had the same electrophoretic mobility as one of the five bands of peptic activity present in the crude extract. The molecular weights of the pepsinogen and the pepsin were 40 000 and 36 000, respectively. Quail pepsin was stable in alkali up to pH 8.5. The optimal pH of the pepsin on hemoglobin was pH 3.0. The pepsin had about half the milk-clotting activity of purified porcine pepsin, but the pepsinogen itself had no activity. The hydrolytic activity of quail pepsin on N-acetyl-L-phenylalanyl-3,5-diiodo-L-tyrosine was about 1% of that of porcine pepsin. Among the various protease inhibitors tested, only pepstatin inhibited the proteolytic activity of the pepsin. The amino acid composition of quail pepsinogen was found to be rather similar to that of chick pepsinogen C, and these two pepsinogens possessed common antigenicity. |
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Authors:
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H Esumi; S Yasugi; T Mizuno; H Fujiki |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 611 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1980 Feb |
Date Detail:
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Created Date: 1980-05-14 Completed Date: 1980-05-14 Revised Date: 2003-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 363-70 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Chickens Coturnix Electrophoresis, Polyacrylamide Gel Enzyme Activation Hydrogen-Ion Concentration Pepsin A / isolation & purification*, metabolism Pepsinogens / immunology, isolation & purification*, metabolism Proventriculus / enzymology* Species Specificity Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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0/Pepsinogens; EC 3.4.23.1/Pepsin A |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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