The attachment of glycolytic enzymes to muscle ultrastructure

Amberson, William R.; Roisen, Fred J.; Bauer, Adelia C.

doi:10.1002/jcp.1030660108

Cited by 45 publications

(9 citation statements)

References 21 publications

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“…The raised serum enzyme reflects abnormal leakage through the muscle cell membrane, CPK being a cytoplasmic rather than a bound mitochondrial enzyme (Amberson, Roisen, and Bauer, 1965). The details of the mechanism of raised serum CPK levels are ununknown; interference in muscle cell energyproducing mechanisms may well be involved (Zierler, 1961).…”

Section: Discussionmentioning

confidence: 99%

Transient acute myositis in childhood.

McKinlay¹,

Mitchell²

1976

Archives of Disease in Childhood

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Section: Discussionmentioning

confidence: 99%

Transient acute myositis in childhood.

McKinlay¹,

Mitchell²

1976

Archives of Disease in Childhood

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“…The use of sucrose as a media was dictated by the knowledge that high concentrations of salt decrease the binding of LDH enzymes to particulate fractions [28]. In addition, the quantitative distribution of enzymes within each particulate fraction is also influenced by the amount of free enzyme that could become bound during the centrifugation procedure itself [6,28,29].…”

Section: Discussionmentioning

confidence: 99%

Cellular Compartmentalization of Lactate Dehydrogenase Isoenzymes

Güttler¹,

Clausen²

1967

Enzymol Biol Clin

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Summary. This investigation describes the quantitative and qualitative distribution of lactate dehydrogenase (LDH) isoenzymes in subcellular particulate fractions of tissues isolated by differential centrifugation. All fractions, especially those containing microsomes and nuclei, had measurable LDH activity. The supernatant remaining after centrifugation of the microsomal fraction contained 40—50% of the total LDH activity and had an isoenzyme pattern similar to that found in the corresponding tissue homogenate. The cathodically migrating LDH isoenzyme, LDH(5) (M(4)), was found mainly in nuclear fractions and the anodically migrating isoenzyme, LDHX (H(4)), in purified mitochondrial fractions. By mixing in vitro equal amounts of nuclear (LDH(5)) and mitochondrial (LDH(4)) fractions, intermediate isoenzyme patterns were obtained containing LDH(2), LDH(3), and LDH(4). If the nuclear and mitochondrial fractions were mixed in a ratio of 10/1 respectively, then the isoenzyme pattern was similar to that seen in malignant tissue in general. The results suggest that changes in the structural elements of the cell, i.e. nuclei and mitochondria, involves changes in the LDH isoenzyme pattern. According to this hypothesis the LDH pattern of malignant tissue is correlated with well-recognized morphologic changes in malignant cells.

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“…In addition to this it may be mentioned that Amberson et al [3,4] by comparing LDH activity in press juice obtained by prolonged ultracentrifugation from rabbit muscle with the total extract of the same muscle suggested an attachment of LDH to ultrastructure of muscle. Also Arnold and Pette [5] reported an adsorption or binding of glycolytic enzymes to structural protein of muscle.…”

Section: Discussionmentioning

confidence: 99%

Extraction and Subcellular Localization of Porcine Lactate Dehydrogenase Activity and Isoenzymes

Hyldgaard‐Jensen

Valenta²

1970

Enzymol Biol Clin

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The conditions for a total extraction of LDH activity and isoenzymes from pig heart, skeletal muscle, liver and spleen were described. Optimal extraction of LDH isoenzymes was obtained by the use of 0.1 M phosphate or tris buffers as extraction media and Ultra-Turrax homogenizer for destruction of tissues. Extraction of isoenzymes mainly composed by M subunits (LDH(5) and LDH(4)) was highly dependent on ionic strength of the homogenizing medium. Maximal release of LDH(2) and LDH(3) was found at a low ionic strength, whereas LDH(1) is independent of ion concentration of extraction medium. The release of cellular LDH isoenzymes by a perfusion of liver confirms the easy removal of LDH(1) and LDH(2) from cells and it is suggested that these isoenzymes exist as free enzymes in situ. Due to certain limitations of techniques available for investigation of the subcellular distribution of LDH isoenzymes, which makes it impossible to differentiate between a true binding of LDH isoenzymes to cell structures or an artificial adsorption to the surface of particles, it is implied that the question about a cellular compartmentalization of LDH isoenzymes still remains unclear. However from the present investigation it is clear that minimally 90 % of LDH is free in Cytoplasma and furthermore that if the remaining 10% is bound or adsorbed at all, the binding is of very loose character and may easily be abolished by the use of a suitable extraction medium.

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The attachment of glycolytic enzymes to muscle ultrastructure

Cited by 45 publications

References 21 publications

Transient acute myositis in childhood.

Transient acute myositis in childhood.

Cellular Compartmentalization of Lactate Dehydrogenase Isoenzymes

Extraction and Subcellular Localization of Porcine Lactate Dehydrogenase Activity and Isoenzymes

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