Nathan L. King

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The hydrothermal isometric tension and thermal transition temperature of collagen were determined in tendons from three different calf muscles. The levels of the nonreducible collagen crosslink, pyridinoline, and the collagen-associated Ehrlich chromogen were also measured in the three tendons. The reducible collagen crosslinks, hydroxylysinonorleucine,(More)
Light-scattering studies on extracts of meat have confirmed the heat-induced breakdown of connectin previously observed by SDS gel electrophoresis. Because of the high subunit MW (∼10(6)) of connectin, the weight-average molecular weight of whole muscle undergoes a relatively large decrease when connectin is broken down during heating of meat. In(More)
Enzymic hydrolysis, followed by amino acid analysis, provided no evidence for the presence of epsilon-(gamma-glutamyl) lysine or other isopeptide crosslinks in connectin. Gel elecrrophoresis in the presence of sodium dodecyl sulphate did not reveal any difference in connectin between normal and lathyritic muscle, indicating that lysyl oxidase does not(More)
Particulates containing a large part of the alkaline phosphatase activity of renal tissue were separated from homogenates and from ribosomal preparations by zonal centrifugation. The particles had a high content of phospholipid and cholesterol that was not removed by treatment with I percent deoxycholate. Enzymatic activities concentrated with the particles(More)
When homogenised muscle (pH 5·5) was heated at 55°C, connectin was extensively degraded, whereas actin and myosin heavy chains were apparently unaffected. It was concluded that carboxyl proteases (e.g. cathepsin D) were largely responsible, because the breakdown of connectin was inhibited by the addition of pepstatin. When whole muscle samples were heated(More)
The rôle of carboxyl proteases in tenderising meat was investigated by injecting the inhibitors, pepstatin and EPNP, into pre-rigor muscle. The increase in shear force values induced by these inhibitors provided a minimum estimate of the extent to which endogenous carboxyl proteases normally tenderise meat at 60°C. Gel electrophoresis showed that connectin(More)
Isoelectric focusing of myofibrillar proteins from raw meat gave one major and several minor actin bands. Extending the time, or raising the temperature, of a heat treatment progressively increased the proportion of variants of isoelectric point lower than the primary component. Because of the concomitant release of ammonia on heating, it was concluded that(More)
Myosin fibres, formed by heat-coagulation under conditions of pH and ionic strength similar to those prevailing in post-rigor meat, exhibited tensile strengths which decreased with fibre diameter. Tensile strengths of the smaller diameter fibres (10-100 μm) ranged from 30 to 3 kg/cm(2). These values resemble breaking strengths reported for cooked meat (e.g.(More)