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Thursday, July 30, 2020 | History

2 edition of Studies on the myosin isoenzymes. found in the catalog.

Studies on the myosin isoenzymes.

David R. W. Welford

Studies on the myosin isoenzymes.

by David R. W. Welford

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  • 30 Currently reading

Published by University of Birmingham in Birmingham .
Written in English


Edition Notes

Thesis (M.Sc) - University of Birmingham, Dept of Biochemistry, 1980.

ID Numbers
Open LibraryOL13737937M

Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or | Explore the latest full-text research PDFs. Cardiac myosins of 10 amphibian species were analysed by electrophoresis. Depending on the species, ventricles and atria contained one or two isomyosins. There were components similar to V2 or V1 of the rat and migrating faster. In the same heart, ventricular and atrial isomyosins were similar or ti .

The immunological studies indicated that human myosins were composed mostly of a V3 type (HV3), but contained also some V1 isomyosin. A technique was developed to quantify the amount of human VI isomyosin which was found to range from almost 0 to 15% of total myosin, and to vary from one heart to the other, regardless of the origin of the heart. Numerous biochemical and pharmacological studies have investigated the specificity and regulatory activity of smooth muscle myosin light-chain phosphatase (MLCP) bound to myosin filaments and comprised of the regulatory myosin phosphatase target subunit 1 (MYPT1) and catalytic protein phosphatase 1cβ (PP1cβ) subunits.

Myosin Isoenzymes of Vascular Smooth and Cardiac Muscle in the Spontaneously Hypertensive and Normotensive Male and Female Rat: A Comparative Study Ingo Morano, Michael Gagelmann, Anders Amer, Ursula Ganten, and Johann Caspar Riiegg Cardiac hypertrophy in hypertensive subjects, its biochemical markers, and functional consequences. The studies are further extended to another species (rat) where the V 1 /V 3 myosin isoenzyme ratio is altered by treating the animal with propyl thiouracil added to the drinking water (PTU); here the contractile protein alteration occurs with myocardial atrophy rather than hypertrophy.


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Studies on the myosin isoenzymes by David R. W. Welford Download PDF EPUB FB2

sarcomeres and capable of deacetylating myosin heavy chain (MHC) isoforms. The motor domains of both cardiac α- and β-MHC isoforms were found to be reversibly acetylated. Biomechanical studies revealed that lysine acetylation significantly decreased the Km for the actin-activated ATPase activity of MHC isoforms.

By inCited by: Myosin isoenzyme distribution and Ca+2-activated myosin ATPase activity in the rat heart is influenced by fructose feeding and triiodothyronine. Dillmann WH.

Studies were conducted to determine if the level of cardiac Ca+2-activated myosin ATPase activity and ventricular myosin isoenzyme distribution are influenced by both T3 administration and Cited by: Reversible lysine acetylation is a widespread post-translational modification controlling the activity of proteins in different subcellular compartments.

We previously demonstrated that a class II histone deacetylase (HDAC), HDAC4, and a histone acetyltransferase, PCAF, associate with cardiac sarcom Cited by: Bouvagnet P, Léger J, Dechesne CA, Dureau G, Anoal M, Léger JJ. Local changes in myosin types in diseased human atrial myocardium: a quantitative immunofluorescence study.

Circulation. Aug; 72 (2)– Lompre AM, Schwartz K, d'Albis A, Lacombe G, Van Thiem N, Swynghedauw B. Myosin isoenzyme redistribution in chronic heart by: Myosin isoenzymes, Ca2+-myosin ATPase activities, and isometric contractile function were measured in cardiac preparations from thyroxine-treated animals and age-matched controls.

Right ventricular hypertrophy did not occur with aging in controls. Thyroxine increased right Studies on the myosin isoenzymes. book weight in each age group compared to the control by: The refinement of the electrophoretic technique in the present study has separated myosin from some specimens of muscle into three isoenzyme forms.

The density of staining of the three myosin bands corresponds to the numbers of muscle fibres staining dark, pale or intermediate grey for ATPase activity after preincubation at pH We have now extended this study to include antibodies prepared against the "head" (S1) and "rod" portions of myosin, as well as the alkali- and 5,5'dithiobis (2-nitrobenzoic acid) (DTNB)-light chains.

Antibodies capable of distinguishing between alkali 1 and alkali 2 type myosin were also used to localize these isoenzymes in the same fast muscle. RABBIT skeletal muscle myosin is composed of two heavy chains and four light chains1. Two classes of light chains can be distinguished both chemically and functionally.

Within the class of. A second interesting finding from this study regards the expression of the Type I MHC This MHC is the same heavy chain as the beta myosin heavy chain found in cardiac myosin and both are encoded for by the same gene (7) The beta MHC is found predominately in the native cardiac myosin isoform designated as V3, and diabetes increases expression.

To define the structural differences that are responsible for the functional diversity between orthologous sarcomeric myosins, we compared the rat and human β/slow myosins. Functional comparison showed that rat β/slow myosin has higher ATPase activity and moves actin filaments at higher speed in in vitro motility assay than human β/slow myosin.

Sequence analysis shows that the loop regions. CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): Myosin is a major component of skeletal muscle and it plays a central role in determining the physiological performance of adult tissue.

Developing muscles contain myosin molecules which are different from the adult forms, and these isoenzymes have been found to be characteristic markers of the diverse physiological.

Because hearts of this age are still undergoing significant maturation, the current study sought to determine if estrogen similarly regulates myosin isoenzyme expression in the mature adult heart. To make this determination, ten month old retired female Sprague-Dawley rats were made estrogen-deficient by ovariectomy (OVAR, n = 8).

Myosin isoenzymes as molecular markers for muscle physiology Article Literature Review (PDF Available) in Journal of Experimental Biology April with 41 Reads. The neonatal myosin heavy chain may be coexpressed with the foetal form and another type, named myosin heavy chain, whose peptide fragments persisted during the rest of the period under study.

A new type of myosin heavy chain, calledis apparently expressed from about 2 years and onwards. DEVELOPMENTAL BIOLOGY() Myosin Isozyme Transitions Occurring during the Postnatal Development of the Rat Soleus Muscle GILLIAN S.

BUTLER-BROWNE AND ROBERT G. WHALEN Departement de Biologic Moleculaire, Institut Pasteur, 25, Rue du Dr. Roux, ^ Paris, France Received ; accepted in revised form November 8, The myosin.

Takeda et al. () studied adaptive changes in two myosin isoenzymes and found small but definite adaptive changes possibly due to long-term ischemia.

Short-term. isoenzyme studies, myosin was dialyzed in 50 mM sodium pyrophosphate buffer containing 50% glyc-erol, 1% 2-mercaptoethanol, and 5 mM dithiothrei-tol (DTT) at pH All procedures were performed at 4°C.

In studies examining isoenzyme distribution in se-lected areas of. Lannergren J. () Contractile properties and myosin isoenzymes of various kinds of Xenopus twitch muscle fibres.

Muscle Res. Cell Motil. 8, Martinez I., Christiansen J. S., Ofstad R. and Olsen R. () Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Lompre AM, Schwartz K, d'Albis A, Lacombe G, Van Thiem N, Swynghedauw B.

Myosin isoenzyme redistribution in chronic heart overload. Nature. Nov 1; ()– Gorza L, Pauletto P, Pessina AC, Sartore S, Schiaffino S. Isomyosin distribution in normal and pressure-overloaded rat ventricular myocardium. An immunohistochemical study.

technique was developed to quantify the amount of human VI isomyosin which was found to range from almost 0 to 15% of total myosin, and to vary from one heart to the other, regardless of the origin of the heart.

Enzymatic studies showed no significant difference between normal. Isoenzymes differ in kinetics (they have different K M and V max values).

Isozymes and allozymes as molecular markers [ edit ] Population genetics is essentially a study of the causes and effects of genetic variation within and between populations, and in the past, isozymes have been amongst the most widely used molecular markers for this purpose.The first evidence for this came from studies of cerebellar Purkinje neurons from dilute mice and rats (Dekker-Ohno et al., ; Takagishi et al., ).

These animals carry null mutations in the myosin Va heavy chain gene and are characterized by a lightened coat color and neurological abnormalities (Mercer et al., ). Smooth ER is.Creatine kinase (CK), CK-MB, lactate dehydrogenase (LDH), LDH-1, troponin T and myosin light chain-1 (MLC-1) were measured.

Abnormal CK-MB elevation was observed in 64% of HCM patients. LDH-1 was not significantly different compared with the control subjects. Troponin T elevation was observed in 3 HCM patients and MLC-1 elevation was not observed.