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SYNTHESIS OF ADENOSINE TRIPHOSPHATE BY MYELIN OF SPINAL NERVES OF RABBIT 1
Author(s) -
Miani N.,
Cavallotti C.,
Caniglia A.
Publication year - 1969
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1969.tb05942.x
Subject(s) - myelin , aldolase a , glucose 6 phosphate isomerase , biochemistry , glycolysis , dehydrogenase , triosephosphate isomerase , lactate dehydrogenase , axolemma , enzyme , chemistry , biology , endocrinology , central nervous system
—1 The myelin fraction isolated by isopycnic gradient centrifugation from rabbit nerve is able to synthesize ATP at substrate level through the Embden‐Meyerhof pathway. Suitable conditions are described to preserve the association of glycolytic enzymes with isolated myelin. 2 Except for phosphofructokinase and ketose‐1‐phosphate aldolase, all the remaining glycolytic enzymes are present in the myelin. A wide divergence was found in the firmness of the association of individual glycolytic enzymes with myelin under the condition of isolation; some, like glucosephosphate isomerase and glyceraldehydephosphate dehydrogenase were retained in high percentage (about 60 per cent of the activity of the homogenate is myelin‐bound); others were weakly bound (no more than 7–6 percent of the lactate dehydrogenase activity of the homogenate is myelin‐bound). 3 By using glyceraldehyde‐3‐phosphate as substrate for glycolysis, about 25 per cent of the total glycolytic activity of rabbit‐nerve homogenate is associated with the myelin. 4 Glucosephosphate isomerase and lactate dehydrogenase may be extracted from and readily recombined with the myelin.