Expressions of hsc/hsp70 cDNAs in bacteria and comparison with tissue-isolated proteins.

Persistent Link:
http://hdl.handle.net/10150/144636
Title:
Expressions of hsc/hsp70 cDNAs in bacteria and comparison with tissue-isolated proteins.
Author:
Zhou, Xiang.
Issue Date:
1993
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
Rat hsc70 and human hsp70 have been expressed in bacteria using the T7 polymerase system. The recombinant proteins, which were the major proteins in E.coli, had the same molecular weights as the tissue-isolated proteins and were immunoactive with hsc70/hsp70 antibodies. ATP binding assay by equilibrium dialysis showed a K$\sb{\rm d}$ for ATP of 0.44 $\mu$M. At saturation, 0.4 mole of ATP was bound per mole of hsc70. Both recombinant and tissue-isolated hsc70/hsp70 have ATPase activities. The denatured substrate, reduced carboxyl methylated $\alpha$-lactalbumin (RCMLA), stimulated ATPase rates of bovine tissue-isolated hsc70/hsp70, but the ATPase rates of rat skeletal muscle and recombinant hsc70 were not changed upon the adding of RCMLA. The analysis of two-dimensional gels showed hsc70/hsp70 isolated from different sources had different isoform patterns. It is speculated that each isoform may have its own substrate specificity.
Type:
text; Thesis-Reproduction (electronic)
Degree Name:
M.S.
Degree Level:
masters
Degree Program:
Animal Sciences; Graduate College
Degree Grantor:
University of Arizona
Committee Chair:
Guerriero, Jr., Vincent

Full metadata record

DC FieldValue Language
dc.language.isoenen_US
dc.titleExpressions of hsc/hsp70 cDNAs in bacteria and comparison with tissue-isolated proteins.en_US
dc.creatorZhou, Xiang.en_US
dc.contributor.authorZhou, Xiang.en_US
dc.date.issued1993en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractRat hsc70 and human hsp70 have been expressed in bacteria using the T7 polymerase system. The recombinant proteins, which were the major proteins in E.coli, had the same molecular weights as the tissue-isolated proteins and were immunoactive with hsc70/hsp70 antibodies. ATP binding assay by equilibrium dialysis showed a K$\sb{\rm d}$ for ATP of 0.44 $\mu$M. At saturation, 0.4 mole of ATP was bound per mole of hsc70. Both recombinant and tissue-isolated hsc70/hsp70 have ATPase activities. The denatured substrate, reduced carboxyl methylated $\alpha$-lactalbumin (RCMLA), stimulated ATPase rates of bovine tissue-isolated hsc70/hsp70, but the ATPase rates of rat skeletal muscle and recombinant hsc70 were not changed upon the adding of RCMLA. The analysis of two-dimensional gels showed hsc70/hsp70 isolated from different sources had different isoform patterns. It is speculated that each isoform may have its own substrate specificity.en_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
thesis.degree.nameM.S.en_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineAnimal Sciencesen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.chairGuerriero, Jr., Vincenten_US
dc.contributor.committeememberHartshone, David J.en_US
dc.contributor.committeememberGoll, Darrel E.en_US
dc.identifier.proquest1353135en_US
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