Plasma alkaline phosphatase isozymes: Isolation and characterization of isozymes
dc.contributor.author | Aminoff, David | en_US |
dc.contributor.author | Austrins, Mikelis | en_US |
dc.contributor.author | Zolfaghari, S. P. | en_US |
dc.date.accessioned | 2006-04-17T16:24:37Z | |
dc.date.available | 2006-04-17T16:24:37Z | |
dc.date.issued | 1971-07-21 | en_US |
dc.identifier.citation | Aminoff, David, Austrins, Mikelis, Zolfaghari, S. P. (1971/07/21)."Plasma alkaline phosphatase isozymes: Isolation and characterization of isozymes." Biochimica et Biophysica Acta (BBA) - Enzymology 242(1): 108-122. <http://hdl.handle.net/2027.42/33605> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GH-47TG2NP-30/2/3bdabb731be8fb033d49b730ae639f76 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/33605 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5001084&dopt=citation | en_US |
dc.description.abstract | 1. 1. The two isozymes of alkaline phosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) detectable in human blood group O plasma have been separated from one another and isolated in a high state of purity. With p-nitrophenyl phosphate as substrate, the catalytic properties of the two isozymes appear to be the same with respect to pH optimum, 10.5; Km, 0.35-0.4 mM, and activity in the presence of EDTA, Mg2+ and Zn2+. The isozymes differ in their electrophoretic mobilities and in their reactivity in the presence of activators and inhibitors. -Phenylalanine specifically inhibits the minor isozyme.2. 2. Comparison of the isozymes isolated from plasmas of individuals of different phenotype indicates that the major isozyme is the same in A, B and O. The minor isozymes of B and O appear to be identical, but they both differ from the minor isozyme detectable in A individuals. Although separable electrophoretically on acrylamide disc electrophoresis and on DEAE-cellulose columns, the minor isozyme from group A individuals appears to have the same catalytic properties as the major component from group A plasma. | en_US |
dc.format.extent | 882357 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Plasma alkaline phosphatase isozymes: Isolation and characterization of isozymes | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Departments of Internal Medicine (Simpson Memorial Institute) and Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationum | Departments of Internal Medicine (Simpson Memorial Institute) and Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationum | Departments of Internal Medicine (Simpson Memorial Institute) and Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.identifier.pmid | 5001084 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/33605/1/0000109.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2744(71)90092-1 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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