Postnatal myosin heavy chain isoform expression in normal mice and mice null for IIb or IId myosin heavy chains Journal Article ...
In the present study we aimed to determine the functional properties and the myosin heavy chain (MHC) isoform composition of single chemically skinned fibres from the vocal muscle of four adult men (age: 55-67 years). Single fibres, dissected from the bioptic samples, were chemically skinned and isometric tension (P0) and maximal shortening velocity (V0) were measured at pCa 4.6. MHC and myosin light chain (MLC) composition of fibre segments and MHC distribution of the biopsy samples were analysed by SDS-poly-acrylamide gel electrophoresis (SDS-PAGE) and densitometry. Four MHC isoforms (1, 2A, 2X and a fourth isoform, provisionally called L) and five MLC isoforms (MLC1s, MLC1f, MLC3f, MLC2f, MLC2s) were identified. The major findings of this study were: (1) fast MHC isoforms (in particular MHC-2A) and fast fibres were predominant, (2) one-third of the fibres were mixed or hybrid, i.e. expressed more than one MHC isoform, (3) V0 and P0 values were determined by the MHC isoform composition and ...
We report the cloning of cDNAs encoding two different human nonmuscle myosin heavy chains designated NMMHC-A and NMMHC-B. The mRNAs encoding NMMHC-A and NMMHC-B are both 7.5 kb in size but are shown to be the products of different genes, which are localized to chromosome 22q11.2 and chromosome 17q13, respectively. In aggreement with previously reported results using avian tissues, we show that the mRNAs encoding the two myosin heavy chain isoforms are differentially expressed in rat nonmuscle and muscle tissues as well as in a number of human cell lines. The cDNA sequence encoding the 5 portion of the NMMHC-A isoform completes the previously published 3 cDNA sequence encoding a human myosin heavy chain, thus providing the cDNA sequence encoding the entire NMMHC-A amino acid sequence. Comparison of this sequence to cDNA clones encoding the amino-terminal one third of the NMMHC-B sequence (amino acids 58-718) shows them to be 89% identical at the amino acid level and 74% identical at the ...
Slow Skeletal Myosin Heavy chain小鼠单克隆抗体可与小鼠, 大鼠, 鸡, 人样本反应并经WB, ELISA, IHC, ICC/IF实验严格验证,被1篇文献引用。
Slow Skeletal Myosin Heavy chain小鼠单克隆抗体[NOQ7.5.4D](ab11083)可与小鼠, 大鼠, 羊, 兔, 山羊, 鸡, 豚鼠, 仓鼠等样本反应并经WB, ELISA, IHC, RIA, EM…
Introduction: We have reported previously that α-myosin heavy chain (α-MyHC) expressing myocytes (MCs), the predominant MC in adult mouse hearts, hypertrophy under pressure-overload without a proportionate increase in total MyHC protein (T-MyHC) content (Lopez et al, Circ. Res., 2011). It is not yet known if during normal physiological growth, these MCs increase their T-MyHC content in proportion to cell size.. Hypothesis: During normal post-natal growth, an increase in T-MyHC content is proportionate to changes in cardiac mass and MC size.. Methods: Individual cardiac cells were isolated by enzymatic digestion from male C57Bl/6 mice age in days 22+/-1 (young, n=4) and 88+/-6 (adult, n=4). Body and heart weights (wt), mean MC volumes by Coulter Multisizer (vol), and cell protein content-per-MC by BCA assay (TotProtMC) were used to measure cardiac growth. A new approach using large-particle fluorescent activated cell sorting (FACS, see Figure) was validated to isolate 15K Troponin-T expressing ...
We have investigated myosin isoform expression during progressive cardiac hypertrophy and the development of congestive heart failure in young male rats. Cardiac enlargement was produced by placing a constricting band (0.024-inch diameter) around the ascending aorta of 25-day-old animals, which resulted in progressively increased stenosis as the rat matured. A 57% and 77% cardiac hypertrophy was observed at 2 and 8 weeks, respectively, with signs of congestive failure at the latter time point. Myosin isoform expression was examined in the subendocardial and subepicardial myocardium of the left ventricle and the free wall of the right ventricle by use of native gel electrophoresis. The percentage of the V3 isoform increased dramatically in both ventricles. In the subendocardial myocardium of the left ventricle, expression of the V3 isoform increased (p less than or equal to 0.05) relative to the subepicardial myocardium at 2, 4, and 8 weeks (17.1% vs. 10.2%, 29.4% vs. 18%, and 46.6% vs. 36.2%). ...
Expression in the adult heart of a number of cardiac genes, including the two genes comprising the cardiac myosin heavy chain locus (Myh), is controlled by thyroid hormone (T3) levels, but there is minimal information concerning the epigenetic status of the genes when their expressions change. We fed mice normal chow or a propyl thio uracil (PTU, an inhibitor of T3 production) diet for 6 weeks, or the PTU diet for 6 weeks followed by normal chow for a further 2 weeks. Heart ventricles from these groups were then used for ChIP-seq analyses with an antibody to H3K4me3, a well-documented epigenetic marker of gene activation. The resulting data show that, at the Myh7 locus, H3K4me3 modifications are induced primarily at 5′ transcribed region in parallel with increased expression of beta myosin heavy chain (MHC). At the Myh6 locus, decreases in H3K4me3 modifications occurred at the promoter and 5′ transcribed region. Extensive H3K4me3 modifications also occurred at the intergenic region between ...
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Assigning DOI numbers, introducing articles from supplements and recent publications to POL-index database, maintaining anti-plagiarism detection, electronic system to proceed manuscripts and webpage of the Journal with interactive pdf files, and language correction of manuscripts published in Journal of Animal and Feed Sciences are financed in the years 2018-2019 by the Ministry of Science and Higher Education from the funds for science popularization activities, Agreement No. 631/P-DUN/2018 ...
Hello - We are doing some studies on the evolution of the muscle myosin heavy chain gene in Drosophila and other insects. We would like to clone the myosin gene(s) from another insect species and are looking for a genomic library from any non-Dipteran insect. If anyone has such a library and is willing to share an aliquot with us we would be tremendously grateful. Please contact me at the email address below. Thanks. Mary Beth Davis University of Pennsylvania School of Medicine Dept. of Cell and Developmental Biology email - davisme at mail.med.upenn.edu ...
Animals were immunized with partially purified human fetal (15 weeks gestation) skeletal muscle myosin heavy chain. Spleen cells were fused with P3X63Ag8.653 mouse myeloma cells.
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Intramuscular triacylglycerols measured by Oil Red O staining combined with an immunofluorescence staining against slow myosin heavy chain (sMHC), to determine
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Monoclonal antibody against Myosin heavy chain (human fast fibers) expressed by MYH2 for use in ELISA, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blot against Bovine, C. elegans, Horse, Human, Llama, Porcine, Quail, Rodent
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Looking for online definition of extraocular muscle myosin heavy chain in the Medical Dictionary? extraocular muscle myosin heavy chain explanation free. What is extraocular muscle myosin heavy chain? Meaning of extraocular muscle myosin heavy chain medical term. What does extraocular muscle myosin heavy chain mean?
The myo2 gene product identified in this study showed similarity to the type II myosin heavy chain in a number of structural features. In addition, Myo2p colocalized with actin overlying mitotic nuclei and could be seen on a shrinking contractile ring. These results strongly suggest that Myo2p composes S. pombe type II myosin, which interacts with actin in the contractile ring and generates force for cytokinesis.. Type II myosin heavy chains known to date carry two IQ motifs, agreeing with the hexameric structure of myosin II. However, we found only one perfect IQ motif (IQXXXRGXXXR) at residues 765-775 in S. pombe Myo2p. A similar sequence to the IQ motif (LQANLQVYNEFR) exists at residues 791-802, but this sequence does not have the central arginine, which is believed to be critical for the binding to the myosin light chain. Thus, we suspect that the type II myosin heavy chain of S. pombe may interact with only one myosin light chain. Interestingly, McCollum et al. (27) observed in their ...
Introduction: The extraocular muscles (EOMs) are considered a separate class of skeletal muscle, allotype. Myosin is the major contractile protein in muscle. The myosin heavy chain (MyHC) isoforms are the best molecular markers of functional heterogeneity of muscle fibers. The relaxation rate, reflects the rate at which Ca2+ is transported back into the sarcoplasmic reticulum (SR) mostly by SR Ca2+ATPase (SERCA). Myosin binding protein C (MyBP-C), plays a physiological role in regulating contraction. The laminins (Ln) are the major non-collagenous components of the basement membrane (BM) surrounding muscle fibers and are important for muscle fiber integrity.. Methods: Adult human EOMs were studied with SDS-PAGE, immunoblots and immunocytochemistry, the latter with antibodies against six MyHC, 2 SERCA, 2 MyBP-C and 8 laminin chain isoforms. The capillary density was also determined.. Results: Most fibers contained a mixture of MyHC isoforms. Three major groups of fibers could be distinguished. ...
Colloidal gold-conjugated monoclonal antibodies were prepared to stage-specific fast myosin heavy chain (MHC) isoforms of developing chicken pectoralis major (PM). Native thick filaments from different stages of development were reacted with these antibodies and examined in the electron microscope to determine their myosin isoform composition. Filaments prepared from 12-d embryo, 10-d chick, and 1-yr chicken muscle specifically reacted with the embryonic (EB165), neonatal (2E9), and adult (AB8) antimyosin gold-conjugated monoclonal antibodies, respectively. The myosin isoform composition was more complex in thick filaments from stages of pectoral muscle where more than one isoform was simultaneously expressed. In 19-d embryo muscle where both embryonic and neonatal isoforms were present, three classes of filaments were found. One class of filaments reacted only with the embryonic antibody, a second class reacted only with the neonatal-specific antibody, and a third class of filaments were ...
The interaction between the calcium-binding protein S100A4 and the C-terminal fragments of nonmuscle myosin heavy chain IIA has been studied by equilibrium and kinetic methods. Using site-directed mutants, we conclude that Ca(2+) binds to the EF2 domain of S100A4 with micromolar affinity and that the K(d) value for Ca(2+) is reduced by several orders of magnitude in the presence of myosin target fragments. The reduction in K(d) results from a reduced dissociation rate constant (from 16 s(-1) to 0.3 s(-1) in the presence of coiled-coil fragments) and an increased association rate constant. Using peptide competition assays and NMR spectroscopy, we conclude that the minimal binding site on myosin heavy chain IIA corresponds to A1907-G1938; therefore, the site extends beyond the end of the coiled-coil region of myosin. Electron microscopy and turbidity assays were used to assess myosin fragment filament disassembly by S100A4. The latter assay demonstrated that S100A4 binds to the filaments and ...
MYH9-related disease (MYH9-RD) is a rare autosomal-dominant disorder caused by mutations in MYH9, the gene for the heavy chain of nonmuscle myosin IIA (NMMHC-IIA). All patients present from birth with macrothrombocytopenia, but in infancy or adult life, some of them develop sensorineural deafness, presenile cataracts, and/or progressive nephritis leading to end-stage renal failure. No consistent correlations have been identified between the 27 different MYH9 mutations identified so far and the variable clinical evolution of the disease. We have evaluated 108 consecutive MYH9-RD patients belonging to 50 unrelated pedigrees. The risk of noncongenital manifestations associated with different genotypes was estimated over time by event-free survival analysis. We demonstrated that all subjects with mutations in the motor domain of NMMHC-IIA present with severe thrombocytopenia and develop nephritis and deafness before the age of 40 years, while those with mutations in the tail domain have a much lower ...
TY - JOUR. T1 - The inhibitory effect of trilinolein on norepinephrine-induced β-myosin heavy chain promoter activity, reactive oxygen species generation, and extracellular signal-regulated kinase phosphorylation in neonatal rat cardiomyocytes. AU - Liu, Ju Chi. AU - Chan, Paul. AU - Chen, Jin Jer. AU - Lee, Horng Mo. AU - Lee, Wen Sen. AU - Shih, Neng Lang. AU - Chen, Yen Ling. AU - Hong, Hong Jye. AU - Cheng, Tzu-Hurng. PY - 2004. Y1 - 2004. N2 - The myocardial protective effects of trilinolein, isolated from the traditional Chinese herb Sanchi (Panax notoginseng),are thought to be related to its antioxidant activity. However, the intracellular mechanism underlying the protective effect of trilinolein in the heart remains unclear. In the present study, we investigated the effect of trilinolein on norepinephrine (NE)-induced protein synthesis in cardiomyocytes. Cultured neonatal rat cardiomyocytes were stimulated with NE, then protein content, [ 3H]-leucine incorporation, and β-myosin heavy ...
Mts1 protein (S100A4 according to a new classification) has been implicated in the formation of the metastatic phenotype via regulation of cell motility and invasiveness. Previously we have demonstrated that Mts1 protein interacted with the heavy chain of nonmuscle myosin in a calcium- dependent manner. To elucidate the role of the Mts1-myosin interaction, we mapped the Mts1-binding region on the myosin heavy chain molecule. We prepared proteolytically digested platelet myosin and a series of overlapped myosin heavy chain protein fragments and used them in a blot overlay with Mts1 protein. Here we report that the Mts1-binding site is located within a 29-amino acid region, at the C-terminal end of the myosin heavy chain (between 1909-1937 amino acids). Two-dimensional phosphopeptide analysis showed that Mts1 protein inhibits protein kinase C phosphorylation of the platelet myosin heavy chain at Ser-1917. We hypothesize that Mts1 protein regulates cytoskeletal dynamics of the metastatic cells ...
Slovenščina (Slovenian). In the present research we tried to prove, that specific myosin heavy chain is relat-ed to a prevalent metabolic type and that activ-ities of succinate-dehydrogenase and a glycerophosphate dehydrogenase in the same fibre types can be different in different muscles. We defined the muscle fibre types (I, IIA and IIB) on transversal sections of frozen muscles accord-ing to their myofibrillar ATPase activity in alka-line and acidic media. We excised extensor digitorum longus, tibialis anterior and diaphragm muscles of five Wistar rats. In the same fibres we immunohistochemically demonstrated myosin heavy chains (MHC) I, IIA, IIB and IIX and histochemically and histophotometrically deter-mined the activities of succinate-dehydrogenase and glycerophosphate dehydrogenase. On the basis of the measured values we differ-entiated fibres in oxydative, glycolytic and oxydative-glycolytic. We found out, that MHC I are present in type I fibres (in extensor digitorum longus muscle ...
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Background: Reversible lysine-acetylation of proteins is regulated by histone acetyl transferases and deacetylases (HDACs). Previous studies from this laboratory have shown that a class-II HDAC, HDAC4 is associated with cardiac sarcomeres, and that HDAC-inhibitors enhance the contractile activity of myofilaments. Since, HDAC4 has little or no deacetylase activity of its own, this study was undertaken to examine the presence of other HDACs on cardiac sarcomeres.. Methods and Results: We prepared skinned papillary muscle fibers of the mouse heart and subjected them to western analysis. Results showed that a class-I HDAC, HDAC3 was localized to cardiac sarcomeres. By immuno-histochemical and electron microscopic analyses we found that HDAC3 was localized to the A-band of cardiac sarcomeres. We therefore examined the reversible acetylation of the A-band protein, myosin heavy chains (MHCs). MHC isoforms were prepared from control and PTU-treated mice, and examined for acetylation by western analysis ...
The purpose of this investigation was to examine the effects of Multiple Sclerosis (MS) on the structural and functional characteristics of skeletal muscle. More specifically, we analyzed the myosin heavy chain (MHC) and fiber type distribution of the vastus lateralis, measured single fiber cross sectional area (CSA), and determined the isokinetic and isotonic strength of the knee extensor muscles. Six sedentary subjects with MS (age: 44 ± 2 yrs) and six sedentary gender-matched controls (age: 46 ± 4) were evaluated. EachMS subject was rated on the Kurtzkes Expanded Disability Status Scale (EDSS) and performed an 8-meter walk test to determine gait speed. Furthermore, the spasticity of the knee extensors was evaluated in each MS subject and weekly energy expenditure was estimated using the Yale Physical Activity Survey. Concentric and eccentric isokinetic strength of the right knee extensors (left in one MS subject) was determined at 60 and 180°/sec and a bilateral isotonic one-repetition ...
Familial hypertrophic cardiomyopathy (FHCM) is an autosomal dominant disease with protean clinical manifestations, ranging from asymptomatic to that of severe heart failure or sudden death. There ist no known parameter in individuals with hypertrophic cardiomyopathy (HCM) that predicts a specific clinical event. This is particularly troublesome for premature sudden death that frequently occurs in young athletes without prior symptoms. Recent identifications of mutations in the beta-myosin heavy chain (betaMHC) gene that co-segregate with the inheritance of the disease provides an opportunity to determine whether certain mutations are more likely to induce a particular clinical event. In this study we analyzed the genotype and phenotype of individuals from two unrelated families with HCM in which the affected individuals have the same missense mutation in exon 13 (G1208A) of the coding sequence for betaMHC. Results: We studied 54 individuals from the two families, 21 were affected with HCM of ...
In smooth muscle cells (SMCs) isolated from rabbit carotid, femoral, and saphenous arteries, relative myosin isoform mRNA levels were measured in RT-PCR to test for correlations between myosin isoform expression and unloaded shortening velocity. Unloaded shortening velocity and percent smooth muscle myosin heavy chain 2 (SM2) and myosin light chain 17b (MLC17b) mRNA levels were not significantly different in single SMCs isolated from the luminal and adluminal regions of the carotid media. Saphenous artery SMCs shortened significantly faster (P | 0.05) than femoral SMCs and had more SM2 mRNA (P | 0.05) than carotid SMCs and less MLC17b mRNA (P | 0.001) and higher tissue levels of SMB mRNA (P | 0.05) than carotid and femoral SMCs. No correlations were found between percent SM2 and percent MLC17b mRNA levels and unloaded shortening velocity in SMCs from these arteries. We have previously shown that myosin heavy chain (MHC) SM1/SM2 and SMA/SMB and MLC17a/MLC17b isoform mRNA levels correlate with protein
Myosin-1, also known as striated muscle myosin heavy chain 1, is a protein that in humans is encoded by the MYH1 gene. This gene is most highly expressed in fast type IIX/D muscle fibres of vertebrates and encodes a protein found uniquely in striated muscle; it is a class II myosin with a long coiled coil tail that dimerizes and should not be confused with Myosin 1 encoded by the MYO1 family of genes (MYO1A-MYO1H). Class I MYO1 genes function in many cell types throughout biology and are single-headed membrane-binding myosins that lack a long coiled coil tail. Myosin is a major contractile protein that converts chemical energy into mechanical energy through the hydrolysis of ATP. Class II Myosins are hexameric proteins composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. Myosin heavy chains are encoded by a multigene family. In mammals, at least ten different myosin heavy chain (MYH) isoforms have been described from striated, smooth, but rarely in ...
inducing hypertrophy". Myosin heavy chain composition of single fibres from m. biceps brachii of male body builders Skeletal muscle hypertrophy and structure and function of skeletal muscle fibres in male body builders Morphological and biochemical evidence of muscle hyperplasia following weight-lifting exercise in rats Morphological observations supporting muscle fiber hyperplasia following weight-lifting exercise in cats The effect of resistive exercise rest interval on hormonal response, strength, and hypertrophy with training. Skeletal muscle hypertrophy and structure and function of skeletal muscle fibres in male body builders http://jp.physoc.org/content/570/3/611.abstract. Needle biopsy samples were taken from vastus lateralis muscle (VL) of five male body builders (BB, age 27.4 ± 0.93 years; mean ±s.e.m.), who had being performing hypertrophic heavy resistance exercise (HHRE) for at least 2 years, and from five male active, but untrained control subjects (CTRL, age 29.9 ± 2.01 ...
Search and download thousands of Swedish university dissertations (essays). Full text. Free. Dissertation: Evolution of MHC Genes and MHC Gene Expression.
To test the quality of the new algorithm, several well-known genes with clusters of mutually exclusive exons with different characteristics were analysed (Figure 3). The first test case is the cytoplasmic dynein heavy chain from Schistosoma mansoni (Sm DHC1). Dynein heavy chains belong to the longest genes in eukaryotes encoding 4000 - 5000 residues and are spread over several dozens of exons. The mutually exclusive exon is clearly identified in the middle of the gene, encoding split codons at the 3- and 5-end of the exon. The query exon and the candidate exon have identical lengths and show strong homology. Based on the multiple sequence alignment of more than 2000 DHCs these exons are mutually exclusive and not constitutive or differentially included. The second case represents the muscle myosin heavy chain gene from the waterflea Daphnia magna[19]. The arthropod muscle myosin heavy chain genes contain several clusters of mutually exclusive exons to fine tune the mechanochemical ...
Myosin-3 is a protein that in humans is encoded by the MYH3 gene. Myosin is a major contractile protein which converts chemical energy into mechanical energy through the hydrolysis of ATP. Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. GRCh38: Ensembl release 89: ENSG00000109063 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000020908 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Eller M, Stedman HH, Sylvester JE, Fertels SH, Rubinstein NA, Kelly AM, Sarkar S (May 1989). "Nucleotide sequence of full length human embryonic myosin heavy chain cDNA". Nucleic Acids Research. 17 (9): 3591-2. doi:10.1093/nar/17.9.3591. PMC ...
FERREIRA, Alexandre y CAMPOS, Gerson Eduardo Rocha. Fiber Type Composition in Semitendinous Muscle of Wistar Rats and Effects of Intermittent Training on its Hypertrophy. Int. J. Morphol. [online]. 2008, vol.26, n.1, pp.63-67. ISSN 0717-9502. http://dx.doi.org/10.4067/S0717-95022008000100010.. Skeletal muscles respond to several stimuli changing their phenotype. Muscular fibers adaptation capability is related to the presence of several myosin heavy chains (MHC). These express four types of pure fibers: I, IIA, IID and IIB containing MHCI, IIa, IId and IIb, respectively. Among pure fibers, there are hybrid fibers, which can express two or more types of myosins. In this study, types of fibers constituting male Wistar rats semitendinous and their myosin heavy chains, as well as influence of intermittent training on hypertrophy of these fibers have been checked through MATPase histochemical technique and electrophoretic proteins separation. All types of pure and hybrid muscular fiber have been ...
Winters LM, Briggs MM, Schachat F (November 1998). "The human extraocular muscle myosin heavy chain gene (MYH13) maps to the cluster of fast and developmental myosin genes on chromosome 17". Genomics. 54 (1): 188-9. doi:10.1006/geno.1998.5558. PMID 9806854 ...
Molecular isoform distribution and glycosylation of acetylcholinesterase are altered in brain and cerebrospinal fluid of patients with Alzheimers disease
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J:21547 Miano JM, Cserjesi P, Ligon KL, Periasamy M, Olson EN, Smooth muscle myosin heavy chain exclusively marks the smooth muscle lineage during mouse embryogenesis. Circ Res. 1994 Nov;75(5):803-12 ...
25 a ON OFF b MUTIPLE CROSS BRIDGES Q) u c S(/) "0 SINGLE CROSS BRIDGE time Fig. 6. A: Diagram of crossbridge cycle. Each crossbridge repeats attachment and detachment cycle. B: Sliding movement of bead driven by single and multiple crossbridges. In summary, we have utilized in vitro motility assay techniques to study the mechanical property of cardiac myosin under various conditions for different myosin isoforms. Although these findings were anticipated based on previous experiments with muscle preparations, this is the first presentation of such direct evidence at the molecular level. 13. J. Thyroxine induced redistribution of isozyme of rabbit ventricular myosin. Circ Res 50: 117 -124, 1982. 14. , et. al. Dynamic interaction between cardiac myosin isoforms modifies velocity of actomyosin sliding in vitro. Circ Res 73:696-704, 1993. 27 15. Barany, M. ATPase activity of myosin correlated with speed of muscle shortening. J Gen Physiol 50:197-218, 1967. 16. , Poggesi, C. et. al. Shortening ...