Glycopeptides derived from individual membrane glycoproteins from control and Rous sarcoma virus-transformed hamster fibroblasts.

Gp, Tuszynski; Baker, S R; Fuhrer, Jürg; Buck, Clayton A.; Warren, Leonard

doi:10.1016/s0021-9258(17)34584-2

Cited by 33 publications

(2 citation statements)

References 22 publications

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“…TG-V, due to the original isolation procedure, came from a variety of external membrane glycoproteins, so it will not be surprising if different amino acids will be found near the oligosaccharide-linkage region. In fact, it has been shown that the glycopeptides characteristic of transformed cells were found on several partially purified glycoproteins therefrom (Van Nest & Grimes, 1977;Tuszynski et al, 1978). The fact that TG-V was from a number of membrane glycoproteins could also account for the difference in specific activity of the fucose recovered after -L-fucosidase treatment of the two fractions (Table II, step 8).…”

Section: Discussionmentioning

confidence: 99%

Partial structure of a membrane glycopeptide from virus-transformed hamster cells

Santer¹,

Glick²

1979

Biochemistry

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The predominant surface glycopeptide from a clone of baby hamster kidney cells transformed by Rous sarcoma virus (C13/B4), metabolically labeled with L-[14C]fucose, has been characterized for the first time. This glycopeptide represents 19% of the total radioactivity removed by trypsin from the cell surface of the transformed fibroblasts and is more abundant in the transformed cells than in the normal counterpart. Purification of the glycopeptide after digestion with Pronase was by successive chromatography on DEAE-cellulose and Sephadex G-50. The monosaccharide content of the glycopeptide was 42, 127, 138, 114, and 243 nmol of fucose, sialic acid, galatose, mannose, and glucosamine, respectively. A partial structure of the glycopeptide was proposed from the results of sequential enzymatic degradation coupled with gas-liquid chromatographic analysis of the resultant monosaccharides. All of the enzymes used were purified and pretested on natural substrates and found to remove terminal monosaccharides of the correct configuration, quantitatively. The purification and properties of an alpha-L-fucosidase from rat testes were described. All of the radioactivity in the glycopeptide, recovered as fucose, was present at the core and was removed by treatment with this alpha-L-fucosidase. The proposed structure is a triantennary, completely sialylated, complex glycopeptide containing a core region of beta-D-mannose, beta-D-N-acetylglucosamine, and alpha-L-fucose.

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Section: Discussionmentioning

confidence: 99%

Partial structure of a membrane glycopeptide from virus-transformed hamster cells

Santer¹,

Glick²

1979

Biochemistry

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“…Trypsinization affords higher yields of glycopeptides than can be obtained by membrane isolation and makes it possible to characterize the oligosaccharide units. Moreover, at least some of the individual glycoproteins have been reported to contain the appropriate species of glycopeptides which characterized them as transformed or nontransformed (Van Nest & Grimes, 1977; Tuszynski et al, 1978).…”

Section: Discussionmentioning

confidence: 99%

Membrane glycopeptides from virus-transformed hamster fibroblasts and the normal counterpart

Glick¹

1979

Biochemistry

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Comparisons of membrane glycopeptides from baby hamster kidney fibroblasts (BHK21/C13) and a clone transformed by Rous sarcoma virus (C13/B4) were made by using cells metabolically labeled with radioactive D-glucose and L-fucose. Most of the glycopeptides were metabolically labeled with both the general and the specific glycoprotein precursors. The glycopeptides obtained from the cell surface by controlled trypsinization were representative of the surface membrane as shown by comparing them with those of purified membrane preparations. The trypsin-removable glycopeptides from both cell types were further processed and examined by successive chromatography on Sephadex G-50 and DEAE-cellulose. The chromatographic distribution patterns showed that each cell type had glycopeptides of similar characteristics, although the proportions of the glycopeptides differed dramatically between the two cell types. After transformation there was an increase in the larger, more highly charged glycopeptides. This was verified by the increased sialic acid content in these glycopeptides. Some of the glycopeptides were homogeneous after the size and charge separations, since a variety of procedures did not separate them further. The apparent homogeneity and reasonably few species obtained may be due to the methods of isolation, with the procedures selecting particular glycopeptides from the external portion of the membrane. These results corroborate the concept and show for the first time that virus transformation is accompanied by an increase in certain species of glycopeptides rather than de novo synthesis.

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Sex differences in blood protein patterns: Two dimensional electrophoretic analysis of the acidic proteins of rat plasma

et al. 1982

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I 1Plasma from normal male and female rats was analyzed, after removal of albumin by affinity chromatography, by two-dimensional electrophoresis. The results demonstrated gender differences in two plasma proteins with apparent molecular weights of 70 000 and 84 000 and isoelectric points ranging from 6.2 to 6.4, and 5.1 to 5.5, respectively. Both proteins were found to be more concentrated in the plasma minus albumin (P-alb) fraction of females than males in both Wistar and Sprague-Dawley rats. The 70000 protein is serum albumin which was more completely removed from male plasma than female plasma. A possible mechanism responsible for this difference is discussed. The results support the existence of "maleness" and "femaleness" in blood protein patterns of rats.

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Glycopeptides derived from individual membrane glycoproteins from control and Rous sarcoma virus-transformed hamster fibroblasts.

Cited by 33 publications

References 22 publications

Partial structure of a membrane glycopeptide from virus-transformed hamster cells

Partial structure of a membrane glycopeptide from virus-transformed hamster cells

Membrane glycopeptides from virus-transformed hamster fibroblasts and the normal counterpart

Sex differences in blood protein patterns: Two dimensional electrophoretic analysis of the acidic proteins of rat plasma

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