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Interactions of smooth muscle and sk...

Sears, Patrick Robert.

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Interactions of smooth muscle and skeletal muscle pyruvate kinases with creatine kinase.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Interactions of smooth muscle and skeletal muscle pyruvate kinases with creatine kinase./
Author:	Sears, Patrick Robert.
Description:	115 p.
Notes:	Adviser: Patrick F. Dillon.
Contained By:	Dissertation Abstracts International61-05B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9971994
ISBN:	0599772255

Interactions of smooth muscle and skeletal muscle pyruvate kinases with creatine kinase.
Sears, Patrick Robert.

Interactions of smooth muscle and skeletal muscle pyruvate kinases with creatine kinase. - 115 p.

Adviser: Patrick F. Dillon.

Thesis (Ph.D.)--Michigan State University, 2000.

Physical and functional coupling of pyruvate kinase (PK) and creatine kinase (CK) has been previously noted with the skeletal enzymes. An isolation procedure was developed for PK from smooth muscle in order to investigate the coupling in this tissue. The coupling of PK with CK in smooth muscle was investigated in relation to the known coupling in the skeletal muscle.

ISBN: 0599772255Subjects--Topical Terms:

1019105
Biophysics, General.

Interactions of smooth muscle and skeletal muscle pyruvate kinases with creatine kinase.
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020 $a 0599772255
035 $a (UnM)AAI9971994
035 $a AAI9971994
040 $a UnM $c UnM
100 1 $a Sears, Patrick Robert. $3 1252898
245 1 0 $a Interactions of smooth muscle and skeletal muscle pyruvate kinases with creatine kinase.
300 $a 115 p.
500 $a Adviser: Patrick F. Dillon.
500 $a Source: Dissertation Abstracts International, Volume: 61-05, Section: B, page: 2524.
502 $a Thesis (Ph.D.)--Michigan State University, 2000.
520 $a Physical and functional coupling of pyruvate kinase (PK) and creatine kinase (CK) has been previously noted with the skeletal enzymes. An isolation procedure was developed for PK from smooth muscle in order to investigate the coupling in this tissue. The coupling of PK with CK in smooth muscle was investigated in relation to the known coupling in the skeletal muscle.
520 $a Kinetic parameters of smooth muscle PK (SMPK) were determined to be similar to those of skeletal PK (SKPK). The Km's for smooth muscle PK were 214 uM ADP and 86 uM PEP. The Km's for skeletal muscle PK were 254 uM ADP and 40 uM PEP. The average Vmax for SKPK was 0.068 U/ug and for SMPK was 0.041 U/ug. Arrhenius plots were linear for both enzymes and the observed activation energy was 61,100 J/mole for SMPK and 56,400 J/mole for SKPK.
520 $a A new method for quantitative measuring of coupling between molecules was developed using capillary electrophoresis (CE). Using these methods it was possible to control the degree of coupling independently by either controlling the concentration of the molecules or the electric field. A CE method was developed for running PK and CK. Qualitative measurements of PK-CK coupling were achieved using the CE methods.
520 $a Procedures which had been previously used for measuring the coupling between the skeletal enzymes were used and adjusted to measure the coupling between the smooth muscle enzymes. These procedures involved the measurement of absorbance changes by the enzymes and changes in their ethanol solubility. A new effect of CK to increase the activity of PK was discovered in the course of these experiments.
520 $a MMCK is the CK isoform. found in skeletal muscle. Smooth muscle has been shown to contain mostly another isoform, BBCK, and some MMCK. The coupling experiments showed that SMPK does not couple with BBCK or MMCK, but that SKPK couples to both. These findings suggest that it may be the isoform of PK that determines PK-CK coupling in different tissues.
520 $a Since glycolytic fluxes in skeletal and smooth muscle are different, the differences in SMPK and SKPK coupling may reflect features of glycolytic flux control which are specific to smooth and skeletal muscle. Using the CE coupling methods the electric field required to uncouple molecules can be determined. The electric field required for dissociation is smaller than that found at distances (0–10 nm) from membranes which are several times larger than the diameter of the enzymes. This suggests that the location of the enzymes at specific sites within the cell may effect their coupling properties.
590 $a School code: 0128.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
690 $a 0786
710 2 0 $a Michigan State University. $3 676168
773 0 $t Dissertation Abstracts International $g 61-05B.
790 $a 0128
790 1 0 $a Dillon, Patrick F., $e advisor
791 $a Ph.D.
792 $a 2000
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9971994