[Various properties of the ceruloplasmin receptor, isolated from human erythrocyte membranes].
An electrophoretically pure preparation of ceruloplasmin (CP) receptor which retains its ability to bind to CP was isolated from human erythrocyte membranes. It was found that in terms of molecular mass, number and size of spontaneously proteolytic fragments as well as antigenicity, the CP receptor molecule strongly resembles that of CP. A comparative analysis of two-dimensional peptide maps of full tryptic digests of the both protein revealed that about 30% of CP peptides are identical in respect of their electrophoretic and chromatographic mobilities which points to the genetic independence of these proteins. The roles of CP and CP receptor in copper metabolism are discussed.
Puchkova
L V
LV
Verbina
I A
IA
Denezhkina
V V
VV
Shavlovskiĭ
M M
MM
Gaĭtskoki
V S
VS
Neĭfakh
S A
SA
D002570:Ceruloplasmin / Q000378:metabolism*; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D008970:Molecular Weight; D010449:Peptide Mapping; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000302:isolation & purification; D011971:Receptors, Immunologic; D018000:Receptors, Peptide; D014357:Trypsin
D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; D018000:Receptors, Peptide; C040519:ceruloplasmin receptor; D002570:Ceruloplasmin; D014357:Trypsin
Nekotorye svoĭstva retseptora tseruloplazmina, vydelennogo iz membran éritrotsitov cheloveka.