ABSTRACT
Histochemical and morphometric parameters of the cricoarytenoideus lateralis muscle of the horse are presented. Using myosin ATPase staining after acid preincubation, 3 fibre types (I, IIA and IIC) were identified. Using NADH-TR staining, type I fibres showed high oxidative capacity, whereas type II fibres had high or low oxidative capacity. The type I to type II ratio was of 35:65. This ratio remained constant in the age range examined. Statistically significant (p < 0.01) differences were found in values for fibre size between groups of horses weighing more than 500 kg and less than 400 kg. Mean area of type II fibres was greater (p < 0.001) than that of type I fibres. There were no significant differences in mean area between left and right muscles in the group of animals with less weight. In contrast, significant differences (p < 0.05) in mean area between left and right muscles were found for type I fibres in the group of animals exhibiting a higher weight. The histographical distribution of fibre type areas was unimodal. Most adult horses showed muscle fibre type grouping in the left muscle.
Subject(s)
Horses/anatomy & histology , Laryngeal Muscles/anatomy & histology , Laryngeal Muscles/enzymology , Age Factors , Animals , Atrophy , Female , Histocytochemistry , Hypertrophy , Male , Myosins/isolation & purification , NADH Tetrazolium Reductase/isolation & purificationABSTRACT
Only three major NADPH-nitrotetrazolium blue (NTB) reductases may be detected in a unique top-ale yeast (Saccharomyces cerevisiae, Narragansett strain), which appears to be of a near anaerobic type with the absence of cytochromes c and a/a3 and the presence of cytochromes P-450 and b5. Two of these three major NADPH-NTB reductases possessed NADH-NTB reductase activity; the third was specific for NADPH and was isolated in this laboratory (Tryon, E., Cress, M. C., Hamada, M., and Kuby, S. A. (1979) Arch. Biochem. Biophys. 197, 104-118) vis. NADPH-cytochrome c reductase (FAD-containing). A description of the isolation procedure is provided for one of these two NADH(NADPH)-NTB reductases, viz. NADH(NADPH)-cytochrome c reductase (FMN-containing), which accounts for about one-half of the total cyanide-insensitive menadione-activated respiration of this yeast. This NADH(NADPH)-cytochrome c reductase has been isolated from an extract of an acetone powder of the top-fermenting ale yeast, with an apparent purification of more than 67-fold and a final specific activity of 0.41 and 0.31 mumol/min/mg for NADH- and NADPH-dependent reduction, respectively. The isolated enzyme proved to be homogeneous by electrophoresis on cellulose acetate and on polyacrylamide gels. It had a pI of 5.25 (at gamma/2 = 0.05) and a molecular size under nondenaturing conditions (as determined by chromatography on Sephadex G-100 and Sephacryl S-200) of 70,000 daltons. On denaturation, the enzyme dissociated into two similar, if not identical, subunits which possessed a molecular weight of 34,000 by sodium dodecyl sulfate/urea-polyacrylamide gel electrophoresis and a weight average molecular weight of 35,000 by sedimentation equilibrium in the presence of 4.0 M guanidinium chloride. The absorbance spectrum of NADH(NADPH)-cytochrome c reductase (FMN-containing) showed three maxima at 464, 383, and 278 nm, with extinction coefficients of 9.88, 9.98, and 64.6 mM-1 cm-1, respectively. The reductase, as isolated, contained 0.63 mol of FMN/34,000-dalton subunit, with no metals and one sulfhydryl group/subunit. Its amino acid composition is reported herein. Anaerobic titrations with dithionite or NAD(P)H revealed a two-electron reduction of FMN, with no spectrally observable semiquinone intermediates.(ABSTRACT TRUNCATED AT 400 WORDS)
Subject(s)
NADPH-Ferrihemoprotein Reductase/metabolism , Saccharomyces cerevisiae/enzymology , Amino Acids/analysis , Fermentation , Flavin Mononucleotide/analysis , Kinetics , Molecular Weight , NAD/metabolism , NADH Tetrazolium Reductase/isolation & purification , NADP/metabolism , NADPH-Ferrihemoprotein Reductase/isolation & purification , Oxidation-Reduction , Oxygen ConsumptionABSTRACT
Mobility patterns of 5 isoenzymes in strains of Tetrahymena pyriformis were demonstrated using polyacrylamide disc gel electrophoresis. Six stock strains were compared in these patterns to 4 strains representative of each of the previously described 4 major "phenotypic sets." Stock strains segregated into predicted "phenosets." and essentially confirmed validity and reproducibility of such a discrimination method. The proposal that new strain designations be assigned on a basis of "phenoset" conformity is reaffirmed.
