LDHk, a uniquely regulated cryptic lactate dehydrogenase associated with transformation by the Kirsten sarcoma virus.

Abstract

A novel isozyme of lactate dehydrogenase is detected in various cells transformed by the Kirsten murine sarcoma virus (KiMSV). This isozyme, designated LDHk, is strongly inhibited by physiological concentrations of oxygen, in an apparently cooperative fashion. LDHk is inhibited by guanosine triphosphate and related compounds, in a noncompetitive fashion. LDHk is found with both 35,000- and 22,000-dalton subunits, although these probably cleave from a 57,000-dalton precursor. In studies utilizing a temperature-sensitive transforming gene mutant of the Kirsten sarcoma virus, we find in vivo expression of LDHk is also temperature-sensitive. In studies using either crude cell-free extracts or purified LDHk, we find the enzyme from cells infected with a temperature-sensitive transforming gene mutant of KiMSV is thermolabile relative to that from wild type KiMSV-infected cells.