Quantitative studies on the interaction of concanavalin A, the carbohydrate-binding protein of the jack bean, with model carbohydrate-protein conjugates
dc.contributor.author | Iyer, R. N. | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.date.accessioned | 2006-04-17T16:39:40Z | |
dc.date.available | 2006-04-17T16:39:40Z | |
dc.date.issued | 1973-05 | en_US |
dc.identifier.citation | Iyer, R. N., Goldstein, I. J. (1973/05)."Quantitative studies on the interaction of concanavalin A, the carbohydrate-binding protein of the jack bean, with model carbohydrate-protein conjugates." Immunochemistry 10(5): 313-322. <http://hdl.handle.net/2027.42/33889> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73FY-4840JMR-GN/2/278a948ca40c08a9bc08b413dd4f75ad | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/33889 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4200120&dopt=citation | en_US |
dc.description.abstract | The interaction of concanavalin A with a comprehensive series of carbohydrate-bovine serum albumin comjugates was investigated by agar gel diffusion and quantitative precipitation techniques. These studies showed that when conjugated to bovine serum albumin, those sugars which inhibited concanavalin A-polysaccharide interaction formed a precipitate with concanavalin A. The unexpected reactivity of the p-phenylazo [ss]--glucopyranoside-bovine serum albumin conjugate is rationalized on the basis of inhibition data employing several aryl and alkylglycosides. | en_US |
dc.format.extent | 779344 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 | Quantitative studies on the interaction of concanavalin A, the carbohydrate-binding protein of the jack bean, with model carbohydrate-protein conjugates | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | 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 | Department of Biological Chemistry, University of Michigan School of Medicine, Ann Arbor, Michigan 48104, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan School of Medicine, Ann Arbor, Michigan 48104, U.S.A. | en_US |
dc.identifier.pmid | 4200120 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/33889/1/0000154.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0019-2791(73)90027-X | en_US |
dc.identifier.source | Immunochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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