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  • 1
    Publication Date: 1963-11-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 2
    Publication Date: 1973-11-01
    Print ISSN: 0145-479X
    Electronic ISSN: 1573-6881
    Topics: Biology , Chemistry and Pharmacology , Physics
    Published by Springer
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  • 3
    Publication Date: 1966-08-01
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 4
    Publication Date: 1973-04-01
    Print ISSN: 0021-9541
    Electronic ISSN: 1097-4652
    Topics: Biology , Medicine
    Published by Wiley
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Endogenous phospholipase A activity was observed to be associated with the microsomal fraction of flounder muscle. Preincubation of microsomes with exogenous phospholipase A 2 resulted in an inhibition of both enzymic and nonenzymic lipid oxidation systems contrary to the generally accepted assumption that fatty acids are more susceptible to oxidation when free than when esterified. Removal of free fatty acids from the membrane led to a partial restoration of oxidative activity in both systems. Preincubation of microsomes with phospholipase C lowered enzymic oxidation but did not affect non-enzymic oxidation, whereas, preincubation with 1% sodium desoxycholate led to inhibition of both oxidation systems. This study suggests a direct role of phospholipid hydrolysis in the inhibition of lipid oxidation in an isolated membrane fraction of fish muscle and the possibility that such hydrolysis in situ may be a controlling factor in lipid oxidation and its subsequent effects.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 42 (1977), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Streptomyces griseus protease was immobilized to porous glass and characterized kinetically. The immobilized protease was then used in a plug flow reactor to inactivate enzymes in solution at low concentrations. The glass-bound protease was effective against fungal glucose oxidase and partially effective against soluble S. griseus protease. Some enzymes were more efficiently inactivated by plain or silanized glass without enzyme, presumably due to adsorption. Less tomato pectin methylesterase was inactivated by glass-bound protease than by plain glass. This is most likely due to masking of adsorption sites by the immobilized protease.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 35 (1970), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY: Skeletal muscle of brown trout contained one electrophoretically distinguishable lactate dehydrogenase (LDH) isozyme. In homogenates of the muscle, release of the enzyme into the soluble phase was favored by high ionic strength and high pH. DPNH solubilized the enzyme and prevented binding of soluble enzyme to particulate matter at concentrations which contributed only negligibly to the ionic strength of the suspending medium. The other compounds involved in the LDH-catalyzed reaction, DPN+, pyruvate, and lactate, were less effective. The effect of the latter two was due chiefly to their contribution to the ionic strength of the medium. Pyruvate, however, used with either DPNH or DPN+ exhibited a synergistic activity. Effective solubilization showed remarkable specificity for DPNH and TPNH. Solubilization by DPNH was also dependent on the tissue concentration of the suspending medium. The lower the tissue concentration, the more readily LDH is solubilized by DPNH. In addition to certain metabolic implications, this information may be used to define assay conditions to allow the study of the kinetics of LDH in bound and soluble forms.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 34 (1969), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY– The outer sheath, or sarcolemma, of the muscle cell plays an important role in the contractile process and may, therefore, be significant in the changes which occur in muscle post-mortem. It has been suggested that a breakdown in a cytoskeleton of the cell is necessary before the contractile proteins become accessible to water and extractable.One procedure for preparing sarcolemmae involves homogenization of the muscle in CaCl2 solution, washing with NaCl-histidine, and an incubation for 30 min at 37°C. Several factors which govern the ability to prepare sarcolemmae from chicken breast muscle largely free of other cellular components have been studied in this report. These include CaCl2 concentrations during homogenization, NaCl and histidine concentrations during the washes, the pH of the wash solutions, the number of washes required, the necessity of the incubation, and the pH of the extracting water.The purpose of these experiments was to find a procedure which would allow variation of the preparatory conditions so that the association of enzymes with the sarcolemma could be studied. It is known that the association of enzymes with particulate fractions of the cell are sensitive to environmental conditions. A necessary step to allow restrictive conditions of preparation, such as low pH and ionic strengths, to be used was aging of the whole excised muscle for 4 hr at 0–4°C. The function of this aging process is not known. It does not appear to involve solubilization of protein nor major changes in several classes of phosphorus compounds.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 34 (1969), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY– Sarcolemmae are usually identified solely by morphological characteristics. We have determined several chemical and enzymic properties of sarcolemmae from chicken breast muscle prepared by homogenization of aged muscle in dilute CaCl2 solution, washing 4 times in NaCl-histidine at pH 7.4, extraction with water buffered to pH 7 and isolation by differential centrifugation on a discontinuous sucrose gradient. The phospholipid content of the sarcolemmae was low, representing only 2 to 3% by weight compared with the 20 to 35% usually found in membraneous systems. This discrepancy may be due to the relatively small proportion of plasma membrane in the sarcolemma.Analyses indicate little contamination by nuclei or mitochondria. The sarcolemmae have, like the microsomal fraction, high contents of RNA and glucose-6-phosphatase activity. The sarcolemma is either rich in these elements or is contaminated by other subcellular elements, such as the transverse tubules (T system), which are. The sarcolemmae display a Mg+2- activated ATPase activity which is typical for membraneous systems. Lactate dehydrogenase was shown to be associated with the sarcolemmae. Whether this represents the situation in vivo or is an artifact of preparation is not clear. The sarcolemmae are capable of binding soluble LDH.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 33 (1968), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Aging of muscle had previously been shown in our laboratory to increase the propensity of properly treated muscle cell segments to empty on extraction with water. It has been suggested that this emptying is caused by breakdown of a cytoskeleton, and, further, that this cytoskeleton is stabilized by flavin adenine dinucleotide (FAD). Due to the possible relationship of cytoskeletal breakdown to quality changes in meat post-mortem, the role of FAD in the preservation of cytoskeletal structure in chicken breast muscle was studied. No significant differences in FAD decomposition or extraction were found between samples handled in a manner such as to produce very large differences in the extent of emptying, the measure of cytoskeletal breakdown. Similarly, adding FAD to suspensions of muscle cell segments could not inhibit emptying under conditions where the supernatant fraction of a muscle homogenate could. It was concluded that FAD plays no role in the stabilization of the cytoskeleton of chicken breast muscle.
    Type of Medium: Electronic Resource
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