토끼 LDH isoenzyme의 특성과 인삼분획이 미치는 영향에 관한 연구

Abstract

Five types of l.1ctate dehydrogenase (LDH) have been identified in mammalian tissues by starch-gel electrophoresis (Markert and M¢ller, 1959), LDH-1 being nearest the anode , and LDH-5 nearest the cathode. It is now well established (Cahn et al. , 1962) that each isoenzyme is composed of four polypeptide chains which are assembled from two different polypeptide units, A and B, as designa• ted by Markert (1961) (M and H by Cahn et al. , 1962). LDH isoenzyme 1 through 5, therefore, have the following polypeptide compositions: AoB4, AjB3, AzBz, A3Bj and A4Bo. Since the synthesis of the A and B polypeptides is controlled by two different genes (Markert, 1963), the phenotypic expression of the LDH isoenzyme pattern of any tissue or cell is known to be dependent on the relative activity of these two genes. The proportions of the LDH isoenzymes have been observed to change during the development of various tissues from rat (Fine, Kaplan and Kuftireclι 1963), chick (Chan et al. , 1962: Nebel and Coklin , 1965). rabbit (Vessell, Philip and Beam, 1962) and human (Fine, Kaplan and Kuftireclι 1963: Latner and Skiller, 1964), which suggests that the two structural genes are under independent but possibly linked control. Attention has been directed chiefly towards liver and skeletal muscle in which the proportions of the more slowly migrating M-containing isoenzymes increase during development, and towards heart where the proportions of H-containing isoenzymes increase during development.