Protein-carbohydrate interaction : On the mode of binding of aromatic moieties to concanavalin A, the phytohemagglutinin of the jack bean
dc.contributor.author | Poretz, R. D. | en_US |
dc.contributor.author | Goldstein, Irwin J. | en_US |
dc.date.accessioned | 2006-04-17T16:22:55Z | |
dc.date.available | 2006-04-17T16:22:55Z | |
dc.date.issued | 1971-10 | en_US |
dc.identifier.citation | Poretz, R. D., Goldstein, I. J. (1971/10)."Protein-carbohydrate interaction : On the mode of binding of aromatic moieties to concanavalin A, the phytohemagglutinin of the jack bean." Biochemical Pharmacology 20(10): 2727-2739. <http://hdl.handle.net/2027.42/33567> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T4P-477GHDK-V0/2/9a3a4a5f01bcb45b79e28fa681ce59dc | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/33567 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5114508&dopt=citation | en_US |
dc.description.abstract | A number of meta-alkylphenyl [beta]--glucopyranosides were synthesized and their ability to inhibit the concanavalin A-polysaccharide system was examined. The binding constants of these compounds as well as other substituted phenyl [amalgamation or coproduct]--glucopyranosides were related to the hydrophobic ([pi]) and electronic ([sigma]) nature of the substituents utilizing the equations devised by Hansch S and Hammett[paragraph sign] respectively.Regression analysis of these relationships revealed that: (1) no linear correlation between the binding constants and the electronic properties of the aromatic substituents was evident; (2) the molecular volume of mono-ortho-substituents does not significantly effect the binding of aromatic [beta]--glucopyranosides to concanavalin A; and (3) the hydrophobic nature ([pi]) of ortho- and meta- but not para-substituents is closely associated with the binding of aryl [beta]--glucosides to concanavalin A.It is proposed that apolar binding involving hydrophobic interactions associated with ortho and meta but not with the para positions of the aromatic nucleus are the predominant forces involved in the binding of the phenyl moiety of phenyl [beta]--glucosides to concanavalin A. | en_US |
dc.format.extent | 1007617 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 | Protein-carbohydrate interaction : On the mode of binding of aromatic moieties to concanavalin A, the phytohemagglutinin of the jack bean | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | 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, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.identifier.pmid | 5114508 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/33567/1/0000068.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-2952(71)90182-1 | en_US |
dc.identifier.source | Biochemical Pharmacology | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.