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Clinical Chemistry 17: 926-930, 1971;
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Clinical Chemistry, Vol 17, 926-930, Copyright © 1971 by the American Association for Clinical Chemistry

Aldolase Isoenzymes in Patients with Progressive Muscle Dystrophy and in Human Fetuses

Elena Tzvetanova 1

1 Department of Neurology, Higher Medical Institute (Director: Professor Sasho Bozhinov), Sofia, Bulgaria.

Aldolase isoenzymes were studied in serum and muscle tissue of normal individuals, 60 patients with different forms of progressive muscle dystrophy (PMD), and 50 patients with other types of neuromuscular diseases. The isoenzyme pattern has been investigated also in the muscle tissue of 30 human fetuses of six to 27 weeks. The isoenzymes were separated in agarose gel. In 40 sera from normals, two isoenzyme fractions were conspicuous, of which A4 was the stronger. In patients with PMD and acute polymyositis with marked hyperaldolasemia, the serum isoenzymogram was also changed. In all other patients with a normal serum aldolase activity, no changes were seen in the serum isoenzymogram. In 25 control muscle, biopsies one isoenzyme fraction, A4, was found. In patients with PMD and other neuromuscular diseases, changes in the muscle isoenzymogram were established, characterized by the appearance of one or two hybrid fractions (A3C + A2C2), and the muscle isoenzymogram resembled that of the fetal muscle. During embryonic development, human muscle tissue changes its isoenzyme pattern. During the earliest stages of development, because of the parallel synthesis of the A and C subunits, five isoenzyme fractions could be observed. In the stages that follow, the isoenzyme patterns showed a shift from C to A. By the end of the embryonic development A4 had become the prevalent form. The normal serum activity originates from muscle origin. Changes in the isoenzyme pattern of the muscle were paralleled by changes in the serum isoenzymogram of the patients with PMD. Significance of the data obtained and the role of regulator-genes is discussed.


Key Words: rases enzymic activity in normal, dystrophic, and fetal muscle and serum • carbohydrate metabolism • gene regulation of isoenzyme production • agarose gel electrophoresis • embryonic development • neuromuscular diseases • isoenzymes

Submitted on May 13, 1971
Accepted on June 11, 1971






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Copyright © 1971 by the American Association for Clinical Chemistry.