Characterization and N-terminal sequence of human platelet proteoglycan.
Human platelet proteoglycan (P.PG) was prepared from a 4 M-guanidinium chloride platelet extract in the presence of proteinase inhibitors. The purification procedure included CsCl-density-gradient centrifugation, DEAE-Sepharose CL-6B ion-exchange chromatography and f.p.l.c. on a Mono Q HR 5/5 column. P.PG was recovered as a polydisperse molecule, but the protein core appeared to be at least 90% homogeneous. This observation could be due to partial proteolysis of the core protein during extraction. The N-terminal sequence of the human P.PG core protein was determined up to residue 66 and was shown to be highly homologous to the propeptide of an embryonic rat yolk-sac tumour proteoglycan (PG19); the significance of this homology is discussed.
Périn
J P
JP
Laboratoire des Protéines (U.A. C.N.R.S. n. 1188), Université de Paris V, France.
Bonnet
F
F
Maillet
P
P
Jollès
P
P
D000595:Amino Acid Sequence; D001792:Blood Platelets / Q000032:analysis*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D011509:Proteoglycans / Q000097:blood* / Q000302:isolation & purification
D011509:Proteoglycans