TY - JOUR
T1 - Lactate dehydrogenases in spermatozoa
T2 - Subunit interactions in vitro
AU - Goldberg, Erwin
N1 - Funding Information:
work was supported Science Foundation.
PY - 1965/1
Y1 - 1965/1
N2 - The sperm-specific lactate dehydrogenase (LDH) isozyme from human, bovine, and murine sources has been dissociated, and its subunits have been recombined with subunits from the other forms of the enzyme. New LDH's are generated and have been characterized on the basis of substrate and coenzyme specificity. The properties of these new molecules are a reflection of their subunit composition, which, in turn, must determine either directly or indirectly the characteristics of the catalytic site(s) of the enzyme. The observations reported here demonstrate that the sperm-specific LDH contains polypeptide subunits which differ from those in LDH 1, 2, 3, 4, and 5.
AB - The sperm-specific lactate dehydrogenase (LDH) isozyme from human, bovine, and murine sources has been dissociated, and its subunits have been recombined with subunits from the other forms of the enzyme. New LDH's are generated and have been characterized on the basis of substrate and coenzyme specificity. The properties of these new molecules are a reflection of their subunit composition, which, in turn, must determine either directly or indirectly the characteristics of the catalytic site(s) of the enzyme. The observations reported here demonstrate that the sperm-specific LDH contains polypeptide subunits which differ from those in LDH 1, 2, 3, 4, and 5.
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U2 - 10.1016/0003-9861(65)90298-5
DO - 10.1016/0003-9861(65)90298-5
M3 - Article
C2 - 14281937
AN - SCOPUS:0343059879
SN - 0003-9861
VL - 109
SP - 134
EP - 141
JO - Archives of biochemistry and biophysics
JF - Archives of biochemistry and biophysics
IS - 1
ER -