Carbohydrate portion of membrane-located mouse H-2 alloantigens

Muramatsu, Takashi; Nathenson, Stanley G.

doi:10.1021/bi00827a008

Cited by 59 publications

(10 citation statements)

References 22 publications

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“…The [3H]fucose radioactivity was eluted between the included and excluded volumes, whereas the [UC]amino acid radioactivity was eluted in the included volume. These findings further confirm that the TL alloantigen fragment is a glycoprotein because the [3H]fucose and [14C]amino acid peak coincided during SDS-Sephadex G-150 (6). The digest was lyophilized, dissolved in 0.7 ml of water, and applied to a Sephadex G-50 fine column (0.9 X 90 cm), which was equilibrated and eluted with 0.01 M Tris-HC1, pH 8.4, containing 0.15 M NaC1.…”

Section: -supporting

confidence: 73%

Some Biochemical Properties of Thymus Leukemia Antigens Solubilized From Cell Membranes by Papain Digestion

Muramatsu

Nathenson

Boyse

et al. 1973

The Journal of Experimental Medicine

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Thymus leukemia (TL) alloantigenic activity was solubilized by papain proteolytic digestion from intact RADA1 tumor cells. If the cells were labeled with amino acids and fucose, the TL alloantigen could be isolated as a doubly labeled glycoprotein fragment by indirect precipitation from the papain digest. This TL glycoprotein fragment was approximately the same mol wt as the papain-digested H-2.4 alloantigen fragment as judged by chromatography on Sephadex G-150 in sodium dodecyl sulfate. The carbohydrate chain of the TL glycoprotein obtained by exhaustive pronase digestion behaved as a glycopeptide of approximately 4,500 mol wt, as compared with the glycopeptide of the H-2.4 alloantigen that had a mol wt of about 3,500. Thus, the TL alloantigen can be solubilized by papain digestion as a glycoprotein fragment similar in mol wt to the H-2 alloantigen glycoprotein fragment. The carbohydrate chain of the TL glycoprotein is larger than the H-2 carbohydrate chain.

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Section: -supporting

confidence: 73%

Some Biochemical Properties of Thymus Leukemia Antigens Solubilized From Cell Membranes by Papain Digestion

Muramatsu

Nathenson

Boyse

et al. 1973

The Journal of Experimental Medicine

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“…For labeling with radioactive sugars, the cells were plated in 10-cm tissue culture dishes. After 24 hr, when the cells reached exponential growth phase, 50 gCi of [6-3H]fucose (10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25) Ci/mmol, Commissariat a l'Energie Atomique) was added to each dish. The cells were cultured for 24 hr, washed once with Earle's solution lacking Mg2+ and Ca2 , and harvested from tissue culture dishes by EDTA (6).…”

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confidence: 99%

Carbohydrate structure and cell differentitation: unique properties of fucosyl-glycopeptides isolated from embryonal carcinoma cells.

Muramatsu¹,

Gachelin²,

Nicolas³

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

150

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“…This result further suggests that the orientation of the Ia molecule on the cell surface is such that the/3 chain is more exposed to the extracellular environment, and may suggest that this chain may be more directly involved in mediating the function of the molecule. This glycopeptide was also similar in size to that isolated from H-2 antigens, but different from those isolated from the vast majority of cell surface glycoproteins [39]. The association of/32 microglobulin (not to be confused with the Ia/3 chain) with the histocompatibility antigens stimulated a search for a similar association of/?2 microglobulin and Ia antigens.…”

Section: General Structural Considerationsmentioning

confidence: 72%