Rapid purification of secretory acid proteinase from Candida albicans and its characterization.
dc.contributor.author | Banerjee, A | en_US |
dc.contributor.author | Ganesan, K | en_US |
dc.contributor.author | Datta, A | en_US |
dc.date.accessioned | 1991-10-01 | en_US |
dc.date.accessioned | 2009-05-27T09:42:57Z | |
dc.date.available | 1991-10-01 | en_US |
dc.date.available | 2009-05-27T09:42:57Z | |
dc.date.issued | 1991-10-01 | en_US |
dc.description.abstract | Secretory acid proteinase from C. albicans was purified from culture supernatant to apparent homogeneity by ion-exchange chromatography. Two isozymes of the proteinase were resolved using a novel chromatofocusing method. The enzyme, which appears to be a glycoprotein, consists of a single polypeptide chain with glutamine at the N-terminus. Its molecular weight is about 45,000 and isoelectric point is pH 4.6. At pH 5, the proteinase is stable at 45 degrees C for at least 15 min. It has a broad substrate specificity. With BSA as a substrate, Km was determined to be 1.6 x 10(-4) M. The enzyme is inhibited by pepstatin and thus is a carboxyl proteinase. It undergoes autocatalytic digestion at or below pH 5.0. The kinetics of induction of proteinase by various proteins are also reported. | en_US |
dc.description.affiliation | Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi. | en_US |
dc.identifier.citation | Banerjee A, Ganesan K, Datta A. Rapid purification of secretory acid proteinase from Candida albicans and its characterization. Indian Journal of Biochemistry & Biophysics. 1991 Oct-Dec; 28(5-6): 444-8 | en_US |
dc.identifier.uri | https://imsear.searo.who.int/handle/123456789/28344 | |
dc.language.iso | eng | en_US |
dc.source.uri | https://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.asp | en_US |
dc.subject.mesh | Amino Acids --analysis | en_US |
dc.subject.mesh | Candida albicans --enzymology | en_US |
dc.subject.mesh | Endopeptidases --isolation & purification | en_US |
dc.subject.mesh | Isoelectric Point | en_US |
dc.subject.mesh | Isoenzymes --isolation & purification | en_US |
dc.subject.mesh | Kinetics | en_US |
dc.subject.mesh | Molecular Weight | en_US |
dc.title | Rapid purification of secretory acid proteinase from Candida albicans and its characterization. | en_US |
dc.type | Journal Article | en_US |
dc.type | Research Support, Non-U.S. Gov't | en_US |
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