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An adipocyte plasma membrane-associated protein kinase has been isolated by use of an anti-phosphotyrosine antibody. The enzyme is present in all cells of the adipose tissue studied, but is absent in red blood cells and most other hematopoietic cells. The protein kinase shows similar properties to the GTP-dependent protein kinase of adipocytes, except that the T4 polynucleotide kinase activity and cellular ATP level are inhibited in the presence of the anti-phosphotyrosine antibody. Phosphorylation/dephosphorylation of the enzyme can modulate activity, and there is an apparent sigmoidal relationship between phosphorylation and kinase activity. This behavior is best described by a hyperbolic function and correlates with the presence of two (alpha and beta) subunits of molecular weight approximately 70,000. Partial resolution of the partially phosphorylated form of the enzyme with polyacrylamide gel electrophoresis shows a third band corresponding to a putative beta subunit (Mr = 73,000). Addition of dithiothreitol or phosphatase to membranes significantly increases the signal obtained by autoradiographic analysis with the anti-phosphotyrosine antibody. It is suggested that the protein kinase which is present in adipocytes is phosphorylated.Chemicals such as hydrocarbons are commonly used in processes to clean workpieces. However, when these processes are used to clean workpieces such as semiconductor wafers, it is important to avoid contamination of the workpieces. For example, a workpiece may be contaminated with microorganisms, such as bacteria or mold spores. In these circumstances, the workpiece may be damaged by the chemicals used in the cleaning process.