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Some species of human leukocyte interferon are glycosylated
Authors:J E Labdon  K D Gibson  S Sun  S Pestka
Institution:1. Department of Biochemistry, Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110 U.S.A.;1. Physiological Chemistry and Pharmacology, Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110 U.S.A.
Abstract:The carbohydrate content of all of the species of human leukocyte interferon (IFN-alpha) which have been derived from patients with chronic myelogeneous leukemia (CML) and purified to homogeneity has now been determined. Amino sugar content was measured by high-performance liquid chromatography and fluorescamine detection of acid hydrolysates of each sample. Two species showed significant amounts of glucosamine. Most of the purified species of leukocyte interferon from a myeloblast cell line were also tested, and two species were found to contain sugar residues. These forms also differed from the CML interferons in that they revealed the presence of greater amounts of galactosamine. The apparent lack of carbohydrate in some of the higher-molecular-weight species of interferon implicated factors other than glycosylation in the molecular weight differences. The results indicate that some species of IFN-alpha are glycosylated to various degrees.
Keywords:To whom correspondence should be addressed  
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