Isozymes of lactic dehydrogenase in human tissues.

نویسندگان

  • E S VESELL
  • A G BEARN
چکیده

The heterogeneity of lactic dehydrogenase (LDH) activity in human serum and erythrocytes has been observed in several laboratories (1-7). If each of the electrophoretically-distinguishable enzymes in serum with LDH activity were derived from different tissues, in disease states involving a single organ the normal pattern of serum LDH activity would be altered according to the type of LDH released from the affected organ. This hypothesis was supported by analysis of sera from patients with myocardial infarction and leukemia (1-7). The results suggested that several tissues had characteristic electrophoretic distributions of lactic dehydrogenase activity. It was concluded that the patterns of serum LDH activity obtained by electrophoresis furnished more information regarding the site of pathology than did an examination of the LDH activity of whole serum (1-3). Furthermore, when several tissues were affected in a generalized disease process, as in hemorrhagic or endotoxic shock, it was found that all of the peaks of LDH activity in serum were elevated (8, 9), in contrast to the selective elevation of certain peaks in conditions involving individual tissues. The term isozyme was proposed by Markert and M0ller to refer to the electrophoretically-distinguishable enzymes with similar substrate specificities (6). The present study demonstrates the heterogeneity of LDH activity in several human tissues and correlates the electrophoretic patterns of LDH activity obtained in tissues with those of sera in certain disease states.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Serum lactic acid dehydrogenase isozyme determination in myocardial infarction.

Introduction The principle of electrophoresis is known to be of great use in today's medicine and an expanding literature on this subject supports this view. Various methods for the electrophoretic separation of charged molecules have been developed in the past 15 years. Immunological and physicochemical studies have further increased knowledge of these electrophoretic fractions. On this princi...

متن کامل

Lactic Dehydrogenase Isozymes

Lactic dehydrogenase isozymes (I-lactate, NAD oxidoreductase), which are key enzymes in glycolysis, have been the object of extensive investigation. Five LDH isozymes have been found. The five isozymes represent the five possible tetramaric combinations of the two polypeptides. Thus, the five tetramers range from LDH-l( H4 ) to LDH -5 ( M4 ), the three hybrid enzymes being H3MI, H2 M2, and H j ...

متن کامل

Genetic Evidence for the Subunit Structure of Lactate Dehydrogenase Isozymes.

The lactate dehydrogenases commonly occur in from one to five molecular forms (isozymes) in the various tissues of an animal species.' By means of zone electrophoresis, characteristic patterns of these isozymes may be demonstrated in each tissue. In adult animals, most tissues contain all five isozymes but in different proportions. Usually, heart muscle exhibits principally the first, or most n...

متن کامل

Pyridine nucleotide-linked dehydrogenases and isozymes of normal rat breast and growing and regressing breast cancers.

Four pyridine nucleotide-linked dehydrogenases, glucose-6phosphate dehydrogenase (G6PDH),3 isocitric dehydrogenase (ICDH), lactic dehydrogenase (LDH), and malic dehydrogenase (MDH), and their isozymes have been studied in the normal virgin rat breast, in the breast of tumor-bearing rats, in the breast cancers themselves, and in these tissues following ovariectomy. Enzyme activity expressed per ...

متن کامل

Multiple forms of lactic dehydrogenase in tissues of the mouse: their specificity, cellular localization, and response to altered physiological conditions.

There is increasing evidence that many enzymes exist in tissues and cells in multiple molecular forms (Markert and Moller, 1959). Of less certainty, however, is the question of differences between these multiple molecular forms in terms of their catalytic and physiological activities. Indeed Markert and Moller felt that these forms, termed isozymes, possessed identical substrate specificities a...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of clinical investigation

دوره 40  شماره 

صفحات  -

تاریخ انتشار 1961