Abstract
Abstract Cell-free fractions from a variety of mammalian tissues can catalyze the addition of carbohydrate to polypeptide (1–5). One of these reports describes the transfer of uridine diphosphate (UDP)-galactose to endogenously present IgG, mediated by the microsomal fraction of rabbit lymph node cells (6). The enzymatic activity appears membrane bound in all cases, and use of detergents (such as Triton X-100) has been necessary for its demonstration. This paper describes initial studies on three distinct glycosyl transferases from a murine myeloma tumor and the partial purification of two of them: a galactosyl and an N-acetyl-glucosaminyl (NAG) transferase. In contrast to some reports by others, these latter two enzymes have been obtained in water-soluble form. An important aspect of our experiments was the use as substrate of mouse IgG from which a substantial portion of the carbohydrate had been removed by enzymatic digestion.
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