Synthetic inhibitors of glucocerebroside [beta]-glucosidase
dc.contributor.author | Hyun, Jung C. | en_US |
dc.contributor.author | Misra, Radhey S. | en_US |
dc.contributor.author | Greenblatt, David | en_US |
dc.contributor.author | Radin, Norman S. | en_US |
dc.date.accessioned | 2006-04-07T16:40:09Z | |
dc.date.available | 2006-04-07T16:40:09Z | |
dc.date.issued | 1975-02 | en_US |
dc.identifier.citation | Hyun, Jung C., Misra, Radhey S., Greenblatt, David, Radin, Norman S. (1975/02)."Synthetic inhibitors of glucocerebroside [beta]-glucosidase." Archives of Biochemistry and Biophysics 166(2): 382-389. <http://hdl.handle.net/2027.42/22140> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DN44VF-MK/2/27bdfd5249ed14ecd45fc6418caa2282 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/22140 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1119798&dopt=citation | en_US |
dc.description.abstract | The glucocerebrosidase of human placenta was studied with various potential inhibitors. Several compounds that resemble the lipoidal product of enzyme action, ceramide, proved to be excellent inhibitors, acting by mixed modes (primarily noncompetitively). These were N-decyl--erythro-3-phenyl-2-amino-l, 3-propanediol and several p-substituted derivatives. These compounds were also highly effective in rat spleen toward glucocerebroside and p-nitrophenyl [beta]-glucoside as substrates. The compounds were inactive toward the analogous enzyme, galactocerebrosidase of rat brain, and were slightly stimulatory toward the rat brain enzyme which makes galactocerebroside. Longer and shorter N-alkyl groups proved to be less effective. Decanoic acid amides of phenylaminopropanediol and related compounds proved to be relatively inert, although some were stimulatory. Deoxycorticosterone [beta]-glucoside was a moderately effective noncompetitive inhibitor and is apparently hydrolyzed by a different glucosidase. p-Nitrophenyl [beta]-glucoside was also a moderately effective inhibitor, acting by mixed modes. p-Chloromercuribenzenesulfonate was a good inhibitor, presumably acting on a sensitive cysteine residue. It is concluded that cerebrosidase contains two sensitive sites, one catalytic and the other allosteric, each containing an important anionic group and able to bind glucosides and ceramide-like compounds. | en_US |
dc.format.extent | 709315 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 | Synthetic inhibitors of glucocerebroside [beta]-glucosidase | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Mental Health Research Institute and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.contributor.affiliationum | Mental Health Research Institute and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.contributor.affiliationum | Mental Health Research Institute and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.contributor.affiliationum | Mental Health Research Institute and Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48104, USA | en_US |
dc.identifier.pmid | 1119798 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/22140/1/0000569.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(75)90401-4 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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