The cohydrolases in human spleen that stimulate glucosyl ceramide [beta]-glucosidase
dc.contributor.author | Iyer, Shankar S. | en_US |
dc.contributor.author | Berent, Susan L. | en_US |
dc.contributor.author | Radin, Norman S. | en_US |
dc.date.accessioned | 2006-04-07T18:37:44Z | |
dc.date.available | 2006-04-07T18:37:44Z | |
dc.date.issued | 1983-10-17 | en_US |
dc.identifier.citation | Iyer, Shankar S., Berent, Susan L., Radin, Norman S. (1983/10/17)."The cohydrolases in human spleen that stimulate glucosyl ceramide [beta]-glucosidase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 748(1): 1-7. <http://hdl.handle.net/2027.42/25084> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T21-47RSC8J-8B/2/ca5318411dbfb856ea742cde1a174648 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/25084 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6615847&dopt=citation | en_US |
dc.description.abstract | A family of [beta]-glucosidase-stimulating proteins (called cohydrolase SPH-I here) was isolated from bovine, Gaucher human and control human spleens. All preparations exhibited a similar pattern of four major electrophoretic bands in polyacrylamide when stained with the cationic dye, Stains-All. The bovine bands migrated more rapidly, while the two types of human cohydrolase migrate very similarly. The two human preparations differend in several respects: the concentration was much higher in Gaucher spleen; the Gaucher factors eluted a little earlier from gel permeation and decyl agarose columns; much more of the cohydrolase was bound by a concanavalin A column; the control bands stained less in gels than the Gaucher bands. Antibodies raised in rabbits to bovine cohydrolase reacted with all three preparations. All four bands evident that the cohydrolases from control and Gaucher spleens are similar in many respects, yet differ in some secondary fashion, possibly in carbohydrate content. It is suggested that Gaucher cohydrolase is formed from normal cohydrolase by the nonenzymatic action of cellular glucose over a period of many years, due to slowed catabolism of the cofactor. | en_US |
dc.format.extent | 842336 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 | The cohydrolases in human spleen that stimulate glucosyl ceramide [beta]-glucosidase | 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 | Mental Health Research Institute (Department of Psychiatry) and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Mental Health Research Institute (Department of Psychiatry) and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Mental Health Research Institute (Department of Psychiatry) and Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.identifier.pmid | 6615847 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/25084/1/0000515.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0167-4838(83)90020-1 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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