Muscles, human

Proteoglycans (from cultured human muscle cells). Separated by ion-exchange HPLC using a Biogel TSK-DEAE 5-PW analytical column. [Harper et al. Anal Biochem 159 150 1986.]... 

Conley, K. E., Blei, M. L., Richards, T. L., et al., 1997. Activation of glycolysis in human muscle in vivo. American Journal of Physiology 273 C306-C315. 

The structure of human muscle fructose-1,6-bisphosphate aldolase, as determined by X-ray crystallography and downloaded from the Protein Data Bank. (PDB ID 1ALD Gamblin, S. J., Davies, G. J., Grimes, J. M., Jackson, R. M., Littlechild, J. A., Watson, H. C. Activity and specificity of human aldolases. J. Mol. Biol. v219, pp. 573-576, 1991.)... 

The process by which yeast breaks down glucose has been carefully studied by biochemists and the way in which this transformation occurs is now known in considerable detail. One of the reasons this process is so interesting is that a nearly identical process takes place in human muscle, in this case to furnish energy needed for muscular activity. 

Bigland, B. Lippold, O.C.J. (1954). Motor unit activity in the voluntary contractions of human muscle. J. Physiol. 125,322-335. 

Bigland-Ritchie, B. (1981). EMG and fatigue of human voluntary and stimulated contractions. In Human Muscle Fatigue Physiological Mechanisms (Porter, R. Whelan, J., eds.), pp. 130-156. Pitman, London. 

Boobis, L., Williams, C., Wootton, S.A. (1982). Human muscle metabolism during brief maximal exercise. J. Physiol. 338, 21-22 (Abstract). 

Costill, D.L., Gollnick, P.D., Jansson, E.D., Saltin, B., Stein, E.M. (1973). Glycogen depletion pattern in human muscle fibers during distance running. Acta Physiol. Scand. 89, 374—383. 

Faulkner, J.A., Claflin, D.R., McCully, K.K. (1986). Power output offast and slow fibers from human skeletal muscles. In Human Muscle Power (Jones, N. L., McCartney, N., McComas, A.J., eds.), pp. 81-94, Human Kinetics, Champaign, IL. 

Sahlin, K., Alvestrand, A., Brandt, R., Hultman, E. (1978). Intracellular pH and bicarbonate concentration in human muscle during recovery from exercise. J. Appl. Physiol. 45,474—480. 

Wiles, C.M. Edwards, R.H.T. (1982). The effect of temperature, ischemia and contractile activity on the relaxation rate of human muscle. Clin. Physiol. 2,485-497. 

Proteins are also important nitrogen compounds. They constitute much of the cell materials, and are present in every type of organism known. In humans, muscle tissue, skin, and hair is mostly protein, about half of the dry weight of our bodies. From a chemical point of view, proteins are polymers of amino acids, alpha amine derivatives of carboxylic acids. Only about 20 different amino acids are actually found in proteins. It is the large number of variations in the protein chain, using only these... 

Kar, N.C. and Pearson, C.M. (1979). Catalase superoxide dismutase, glutathione reductase and thiobarbituric acid-reactive products in normal and dystrophic human muscle. Clin. Chim. Acta 94, 277-280. 

Phosphofructokinase (PFK) is a key regulatory enzyme of glycolysis that catalyzes the conversion of fructose-6-phosphate to fructose-1,6-diphosphate. The active PFK enzyme is a homo- or heterotetrameric enzyme with a molecular weight of 340,000. Three types of subunits, muscle type (M), liver type (L), and fibroblast (F) or platelet (P) type, exist in human tissues. Human muscle and liver PFKs consist of homotetramers (M4 and L4), whereas red blood cell PFK consists of five tetramers (M4, M3L, M2L2, ML3, and L4). Each isoform is unique with respect to affinity for the substrate fructose-6-phosphate and ATP and modulation by effectors such as citrate, ATP, cAMP, and fructose-2,6-diphosphate. M-type PFK has greater affinity for fructose-6-phosphate than the other isozymes. AMP and fructose-2,6-diphosphate facilitate fructose-6-phosphate binding mainly of L-type PFK, whereas P-type PFK has intermediate properties. 

N1. Nakajima, H., Noguchi, T., Yamasaki, T Kono, N., Tanaka, T and Tarui, S Cloning of human muscle phosphofructokinase cDNA. FEBS Lett. 223, 113-116 (1987). 

Itani SI, Ruderman NB, Schmieder F and Boden G. 2002. Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IkappaB-alpha. Diabetes 51(7) 2005-2011. 

Tsouloufis et al.8 used an ELISA to assess the refolding of a recombinant subunit of the extracellular domain of the human muscle acetylcholine receptor expressed in E. coli. The plates were coated with refolded or unfolded protein and then reacted with conformationally dependent MAbs. The use of specific... 

Tsouloufis, T., A. Mamalaki, M. Remoundos, and S.J. Tzartos (2000). Reconstitution of conformationally dependent epitopes on the N-terminal extracellular domain of the human muscle acetylcholine receptor alpha subunit expressed in Escherichia colt implications for myasthenia gravis therapeutic approaches. Int Immunol 12(9) 1255-1265. 

Spectroscopic relaxometry performed in human muscles of the lower leg is described in the following sections. 

The flux through the Krebs cycle can be estimated from the oxygen consumption of a cell or tissue. This has been done in a single human muscle during maximum physical... 

When a human muscle, which comprises exclusively anaerobic (i.e. type II6) fibres is physically active, glycogen conversion to lactate generates all the ATP that is required to support the activity. Type I or Ila fibres use this process only when the demand for ATP exceeds that which can be generated from aerobic metabolism, e.g. during hypoxia. The significance of fhese processes for generation of ATP by muscle during various athletic events is discussed in Chapter 13. 

Type 11b fibres in human muscle are different from the rat and sometime known as type llx (Chapter 13). 

Box 9.4 Maximum capacity of the Krebs cycle in invertebrate muscles versus that in human muscle... 

Table 13.2 Properties of human muscle fibre types and their capacities for fuel utilisation ...

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