TY - JOUR
T1 - Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure
AU - Capra, J. D.
AU - Vitetta, E. S.
AU - Klein, J.
PY - 1975
Y1 - 1975
N2 - The murine Ss protein has been isolated and purified. Using specific antisera, the radiolabeled protein has a mol wt of 120,000 in sodium dodecyl sulfatepolyacrylamide gels. It is composed of two basic subunits of 23,000 and 14,000 daltons. The smaller molecular weight subunit contains a single disulfide bridge, is devoid of carbohydrate, and may represent the murine equivalent of β2 microglobulin.
AB - The murine Ss protein has been isolated and purified. Using specific antisera, the radiolabeled protein has a mol wt of 120,000 in sodium dodecyl sulfatepolyacrylamide gels. It is composed of two basic subunits of 23,000 and 14,000 daltons. The smaller molecular weight subunit contains a single disulfide bridge, is devoid of carbohydrate, and may represent the murine equivalent of β2 microglobulin.
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U2 - 10.1084/jem.142.3.664
DO - 10.1084/jem.142.3.664
M3 - Article
C2 - 809530
AN - SCOPUS:0016826221
SN - 0022-1007
VL - 142
SP - 664
EP - 672
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
IS - 3
ER -