TY - JOUR
T1 - Purification and Partial Characterization of Mouse Hemopexin (Beta 2-III Globulin)
AU - Witz, I.
AU - Gross, J.
N1 - Funding Information:
The work was supported in part by the Adolf Friedmann Endowment, and by grants from the Junior Kielcer Aid Society, Chicago.
PY - 1965/4
Y1 - 1965/4
N2 - A method for purification of mouse Beta 2-111 globulin is described. The purified protein is perchloric acid soluble and contains hexose, hexosamine and sialic acid. It is soluble in rivanol and binds hematin. It has a sedimentation constant of 4.3 S, indicating a molecular weight of about 65,000. It is suggested that this protein henceforth be called mouse hemopexin.
AB - A method for purification of mouse Beta 2-111 globulin is described. The purified protein is perchloric acid soluble and contains hexose, hexosamine and sialic acid. It is soluble in rivanol and binds hematin. It has a sedimentation constant of 4.3 S, indicating a molecular weight of about 65,000. It is suggested that this protein henceforth be called mouse hemopexin.
UR - http://www.scopus.com/inward/record.url?scp=78651168463&partnerID=8YFLogxK
U2 - 10.3181/00379727-118-30029
DO - 10.3181/00379727-118-30029
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AN - SCOPUS:78651168463
VL - 118
SP - 1003
EP - 1006
JO - Experimental Biology and Medicine
JF - Experimental Biology and Medicine
SN - 1535-3702
IS - 4
ER -