Persistent Link:
http://hdl.handle.net/10150/184604
Title:
Biochemical properties of caldesmon.
Author:
Abougou, Jean-Claude
Issue Date:
1988
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:
An attempt to develop a short and reliable method of caldesmon purification led to the development of three procedures of caldesmon purification. The first method was seldom used because of its low yield and the lack of caldesmon endogenous kinase activity. However, it allowed us to purify MLCK (myosin light chain kinase). The second and third methods gave respectively, a caldesmon sample with and without kinase activity. We were able to localize the endogenous kinase in the 0-30% ammonium sulfate precipitated DEAE pellet but we were unsuccessful at purifying the kinase to homogeneity. We found that caldesmon can also be phosphorylated by rat brain Ca²⁺-calmodulin-dependent kinase II at sites identical to those of caldesmon endogenous kinase but different to those of kinase C. In addition, caldesmon and its endogenous kinase are two different proteins. Furthermore, our study of caldesmon inhibition of actomyosin ATPase activity showed that further research needs to be done to refute F-actin bundling process as a possible cause of caldesmon inhibition of actomyosin ATPase activity. In addition, our studies of caldesmon inhibition of HMM and S-1 ATPase activity suggest that S-2 might be partially involved in the inhibition mechanism. Finally, caldesmon did not affect the 6S-10S transition of myosin conformation and since caldesmon cannot compete against higher affinity calmodulin-binding protein such as MLCK thus, the flip-flop theory is untenable.
Type:
text; Dissertation-Reproduction (electronic)
Keywords:
Proteins -- Separation.; Calcium-binding proteins.
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Nutritional Sciences; Graduate College
Degree Grantor:
University of Arizona
Advisor:
Allen, Ronald E.; Hartshorne, David J.

Full metadata record

DC FieldValue Language
dc.language.isoenen_US
dc.titleBiochemical properties of caldesmon.en_US
dc.creatorAbougou, Jean-Claudeen_US
dc.contributor.authorAbougou, Jean-Claudeen_US
dc.date.issued1988en_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.abstractAn attempt to develop a short and reliable method of caldesmon purification led to the development of three procedures of caldesmon purification. The first method was seldom used because of its low yield and the lack of caldesmon endogenous kinase activity. However, it allowed us to purify MLCK (myosin light chain kinase). The second and third methods gave respectively, a caldesmon sample with and without kinase activity. We were able to localize the endogenous kinase in the 0-30% ammonium sulfate precipitated DEAE pellet but we were unsuccessful at purifying the kinase to homogeneity. We found that caldesmon can also be phosphorylated by rat brain Ca²⁺-calmodulin-dependent kinase II at sites identical to those of caldesmon endogenous kinase but different to those of kinase C. In addition, caldesmon and its endogenous kinase are two different proteins. Furthermore, our study of caldesmon inhibition of actomyosin ATPase activity showed that further research needs to be done to refute F-actin bundling process as a possible cause of caldesmon inhibition of actomyosin ATPase activity. In addition, our studies of caldesmon inhibition of HMM and S-1 ATPase activity suggest that S-2 might be partially involved in the inhibition mechanism. Finally, caldesmon did not affect the 6S-10S transition of myosin conformation and since caldesmon cannot compete against higher affinity calmodulin-binding protein such as MLCK thus, the flip-flop theory is untenable.en_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.subjectProteins -- Separation.en_US
dc.subjectCalcium-binding proteins.en_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineNutritional Sciencesen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorAllen, Ronald E.en_US
dc.contributor.advisorHartshorne, David J.en_US
dc.contributor.committeememberSunde, Rogeren_US
dc.contributor.committeememberGoll, Darrel E.en_US
dc.identifier.proquest8907949en_US
dc.identifier.oclc701908164en_US
All Items in UA Campus Repository are protected by copyright, with all rights reserved, unless otherwise indicated.