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At least 19 recordsLinked to original sources
PubMed1979

Turnover of pegeon breast muscle pyruvate dehydrogenase complex.

The pigeon breast muscle pyruvate dehydrogenase complex was resolved into three component enzymes: lipoate acetyltransferase, pyruvate dehydrogenase, and lipoamide dehydrogenase. The antibodies against each component enzyme were prepared. All of the antibodies against component enzymes precipitated the pyruvate dehydrogenase complex. The enzyme complex was recovered as the immunoprecipitate from the extract of breast muscle of a pigeon that had received a single injection of L-[4,5-3H]leucine. The immunoprecipitate was separated into each component enzyme by SDS-polyacrylamide gel electrophoresis. The relative isotopic leucine incorporations per mg of protein into each component enzyme 4 h after the injection were 1.0 : 0.9 : 1.4 : 2.7 for lipoate acetyltransferase, alpha- and beta-subunit of pyruvate dehydrogenase, and lipoamide dehydrogenase, respectively. The half-lives of lipoate acetyltransferase, alpha- and beta-subunit of pyruvate dehydrogenase, and lipoamide dehydrogenase were 7.7, 2.5, 2.6, and 1.8 days, respectively. These results indicate that the component enzymes of the pyruvate dehydrogenase complex were synthesized and degraded at different rates.

Animals↗
PubMed1978

Effects of age, sex and starvation on the turnover of plasma, liver and breast muscle proteins in the Japanese quail.

Half-lives of the plasma, liver and breast muscle proteins in female, old male, young male and starved young male Japanese quail were measured by following the changes in protein specific radioactivity over a period of 7 days. The female birds showed the shortest half-lives for plasma and liver proteins and very long half-lives for breast muscle proteins. Compared to the proteins from the female birds, the old and young male birds showed slightly longer half-lives for plasma and insoluble liver proteins and shorter half-lives for soluble liver and breast muscle proteins. Starved birds showed greatly increased half-lives for all proteins when compared to the corresponding proteins from the other groups of quail. In general, the trends shown for the turnover of proteins from plasma, liver and breast muscle of the four groups of quail were similar to turnovers reported for rats under similar treatment conditions.

Aging↗
PubMed1977

[Isolation and some properties of protein kinase from pigeon breast muscle].

Protein kinase was isolated from pigeon breast muscle. The preparation obtained was chromatographically homogeneous. The apparent Km varlue for histone H1 and ATP were 3,5-10(-5) M and 1,6-10(-5) M respectively. The purified enzyme displays high specificity for the lysine-rich histones (H1, H2b, H2a). The protein kinase activity is stimulated, 1,6-fold by cyclic AMP.

Animals↗
PubMed1978

Atrophy of a breast muscle with a single fibre type (M. pectoralis) in fasting willow grouse, Lagopus lagopus (L.).

The willow grouse (Lagopus lagopus) are arctic gallinaceous birds with small fat stores and large muscles. In winter, these birds may starve for periods of several days. It was important to know which energy reserves were utlized during periods of starvation. Body composition of female willow grouse and Bantam hens was studied before and after fasting. Grouse have much larger breast muscles than do Bantams, but reproductive organs are larger in hens. The relative amounts of adipose tissue are about equal in grouse and Bantams. When the birds had lost about 20% of their initial body weight due to fasting, Bantams had lost as much weight from their reproductive organs as from the adipose tissue, with little loss from the muscles. Grouse lost more weight from the pectoralis muscles alone than from the adipose tissue. Since the major component of muscle is protein, the grouse obtain a larger proportion of acloric needs during fasting from protein than do the Bantams. Grouse breast muscles are dark red, and the pectoralis consists homogeneously of type IIa (oxidative-glycolytic) fibres, assessed by ATPase and by Sudan Black staining. The supracoracoideus muscle has type II fibres, not resolvable in subtypes. The leg muscle biceps femoris contains the three fibre types I, IIa, and IIb. During fasting, the weight loss of the pectoralis muscle may be accounted for by all fibres losing some material.

Animals↗
PubMed1976

Studies on phosphoglyceromutase from chicken breast muscle: number and reactivity of sulfhydryl groups.

Phosphoglyceromutase (PGM) from chicken breast muscle was titrated with p-mercuribenzoate (PMB), 5,5'-dithiobisnitrobenzoate (Nbs2), N-ethylmaleimide (NEM), iodoacetate and iodoacetamide. The effect of all of the sulfhydryl reagents, with the exception of NEM was to cause a loss in enzymatic activity. Addition of KCN following reaction with Nbs2 resulted in the recovery of a small amount of enzymatic activity. In the absence of substrate (3-phosphoglyceric acid) or cofactor (2,3-diphosphoglyceric acid) and in the presence or absence of 6 M guanidine hydrochloride, six sulfhydryl groups per mole of enzyme were titrated with PMB.

Amino Acids↗
PubMed1979

[Regulation of alpha-ketoglutarate dehydrogenase complex from pigeon breast muscle].

The activity of alpha-ketoglutarate dehydrogenase complex from pigeon breast muscle is controlled by ADP and the reaction products, i. e. succinyl-CoA and NADH. ADP activates the alpha-ketoglutarate dehydrogenase component of the complex, whereas NADH inhibits alpha-ketoglutarate dehydrogenase and lipoyl dehydrogenase. In the presence of NADH the kinetic curve of the complex with respect to alpha-ketoglutarate and NAD and the dependence of upsilon versus [NAD] and upsilon versus [Lip (SH)2] in the lipoyl dehydrogenase reaction are S-shaped. In the absence of inhibitor ADP had no activating effect on lipoyl dehydrogenase; however, in the presence of NADH ADP decreases the cooperativity for NAD. The cooperative kinetics of the constituent enzymes of the complex are indicative of its allosteric properties. Isolation of the alpha-ketoglutarate dehydrogenase complex and its lipoyl dehydrogenase and alpha-ketoglutarate dehydrogenase components in a desensitized state confirms their allosteric nature. It is assumed that NADH effects of isolated alpha-ketoglutarate dehydrogenase is due to a shift in the equilibrium between different oligomeric forms of the enzyme.

Adenosine Diphosphate↗
PubMed1978

[Separation of catalytic and regulatory subunits of pigeon breast muscle protein kinase].

The separation of catalytic cAMP-independent and regulatory cAMP-binding subunits of pigeon breast muscle protein kinase was performed after the treatment of the holoenzyme by cAMP. The molecular weight of the homogeneous catalytic subunit is determined as 30,000. When catalytic and regulatory subunits were mixed, the decrease of phosphotransferase activity was observed.

Animals↗
PubMed1978

The effect of lipid peroxidation on the calcium-accumulating ability of the microsomal fraction isolated from chicken breast muscle.

The effect of lipid peroxidation on the Ca2+-accumulating and Ca2+-retaining abilities of the microsomal fraction from chicken breast muscle was investigated. At 25 degrees C, enzymic lipid peroxidation did not seriously affect either of these abilities unless ascorbic acid was present, when both were diminished. At 37 degrees C, Ca2+-concentrating ability was decreased further by the effects of heat damage to the membrane. Membrane lipid peroxidation did not affect microsomal adenosine triphosphatase activity unless the microsomal fraction was subsequently washed with albumin. This effect of albumin is possibly due to removal of lipid-breakdown products. Addition of soya-bean phospholipids to the peroxidized vesicles washed with albumin restored adenosine triphosphatase activity, demonstrating a non-specific phospholipid requirement.

Adenosine Triphosphatases↗
PubMed1979

[Some properties of the catalytic subunit of adenosine 3':5'-monophosphate-dependent protein kinase from pigeon breast muscle].

A method for the preparation of a homogenous catalytic subunit of adenosine 3':5'-monophosphate-dependent protein kinase from pigeon breast muscle was developed. The molecular weight of the enzyme as determined by electrophoresis in the presence of sodium dodecyl sulfate was found to be 42000. The pH optimum of the catalytic subunit was around 8.0. The active site of the catalytic subunit was studied using some derivatives of ATP, containing different reactive groups in the triphosphate chain of the molecule. It may be assumed that the pH optimum of the enzyme inactivation by adenosine 5'-chloromethylpyrophosphonate and the protective effect of ATP suggest covalent binding of the imidazole ring in the enzyme active site. The kinetic mechanism of the protein kinase reaction was studied using the initial rate experiments and reaction product inhibition. The results obtained were consistent with a random Bi-Bi kinetic mechanism.

Animals↗
PubMed1977

Studies on phosphoglyceromutase from chicken breast muscle: chemical modification of lysyl residues.

To examine the role of lysyl residues in the activity of the enzyme, phosphoglyceromutase (PGM) from chicken breast muscle was chemically modified with trinitrobenzenesulfonate (TNBS) and pyridoxal 5'-phosphate. Trinitrophenylation resulted in modification of about nine lysines per mole of PGM with almost complete activity loss. Substrate (3-PGA) offered some protection to TNBS inactivation but cofactor (2,3-DPGA) did not. Reduction of the Schiff's base complex between pyridoxal 5'-phosphate and PGM gave irreversible inactivation of the enzyme. Inactivation was due to incorporation of 1 mol of pyridoxal 5'-phosphate per mole of PGM dimer through the epsilon-amino group of a lysyl residue. The effect of pyridoxal 5'-phosphate was specific for intact native enzyme and reaction with only one lysine per dimer was not due to induced conformational changes nor to dissociation of the reacted enzyme. 3-PGA prevented much of the reaction with pyridoxal 5'-phosphate with preservation of 70% of the activity and was a competitive inhibitor of the active site directed reagent. Cofactor (2,3-DPGA) acting noncompetitively, reduced the rate at which inactivation occurred with pyridoxal 5'-phosphate. Incorporation of 2,3-[32P]DPGA into PGM irreversibly inactivated with pyridoxal 5'-phosphate and NaBH4 was incomplete indicating hindrance to phosphorylation in the modified enzyme. The results indicate that a lysyl residue is located at or near the active site of PGM and that it is probably involved in the binding of 3-PGA.

Animals↗
PubMed1979

Influence of ante- and peri-mortem factors on biochemical and physical characteristics of turkey breast muscle.

The course of post-mortem breakdown of glycogen and ATP in turkey pectoralis major muscle was markedly influenced by several ante- and peri-mortem variables. Application of a proper stunning procedure was highly effective in preventing peri- and post-mortem muscle stress reactions. The physiological level of glycogen and ATP was not significantly affected by road transportation covering 260 km. Birds which rested for 24 hrs following transportation had lower glycogen and ATP levels at the moment of slaughter than non-rested birds. According to the changes in the rate and extent of post-mortem biochemical reactions, several meat characteristics such as water-holding capacity, colour, and tenderness were significantly changed. Furthermore, the results also indicate that turkey breast muscle is susceptible to a PSE-like condition as described in pork.

Adenosine Triphosphate↗
PubMed1978

Phosphoglycerate mutase. Kinetics and effects of salts on the mutase and bisphosphoglycerate phosphatase activities of the enzyme from chicken breast muscle.

The steady state kinetics and effects of salts on chicken breast phosphoglycerate mutase have been examined. The enzyme can catalyze three phosphoryl transfer reactions: mutase, bisphosphoglycerate phosphatase, and bisphosphoglycerate synthase. The mutase rate was measured in the favorable direction (Keq = glycerate-3-P/glycerate-2-P approximately equal to 12) using [2T]glycerate-2-P as substrate. The bisphosphoglycerate phosphatase activity was studied in the presence of the activator, glycolate-2-P. The latter is an analog of the glycerate-P's and appears to act as an abortive mutase substrate. The kinetic pattern obtained with both activities is that of a ping-pong mechanism with inhibition by the second substrate occurring at a lower concentration than the Km value for that substrate. The kinetic parameters for the mutase determined in 50 mM N-[tris(hydroxymethyl)methyl-2-amino]ethanesulfonate (TES)/sodium buffer containing 0.1 M KCl, pH 7.5, 25 degrees C are: Km glycerate-2,3-P2, 0.069 micron; Km glycerate-2-P, 14 micron; Km glycerate-3-P approximately 200 micron; Ki glycerate-2-P, 4 micron. The kinetic parameters for the phosphatase reaction in 50 mM triethanolamine/Cl- buffer, pH 7.5, 25 degrees C are: Km glycerate-2,3-P2, 0.065 micron:Km glycolate-2P, 479 micron; Ki glycolate-2-P, 135 micron. The enzyme is sensitive to changes in the ionic environment. Increasing salt concentrations activate the phosphatase in the presence of glycolate-2-P by decreasing the apparent Km of glycerate-2,3-P2. The effects are due to the anionic component and Cl- greater than acetate greater than TES. The same salts are competitive inhibitors with respect to glycolate-2-P. With high levels of KCl that produce a 30-fold decrease in the apparent maximal velocity due to competition with glycolate-2-P, the Km of glycerate-2,3-P2 remains low. These observations lead us to postulate that each monophosphoglycerate substrate has a separate site on the enzyme and that glycerate-2,3-P2 can bind to either site. The binding of anions to one site of the nonphosphorylated enzyme allows an increase in the on and off rates of glycerate-2,3-P2 at the alternate site. Salts inhibit the mutase reaction. The Km of glycerate-2,3-P2 is increased as is that of glycerate-2-P. The effect on the Km of glycerate-2,3-P2 is attributed to an increase in the off rate/on rate ratio for glycerate-2,3-P2. The bisphosphoglycerate synthase reaction is shown to require added glycerate-3-P. The equilibrium between enzyme and glycerate-1,3-P2 is favorable (Kdiss less than or equal 7 X 10(-8) M) and suggests that in the absence of a separate synthase this reaction may have functional significance.

Animals↗