Characterization of goat plasma vitronectin.
Vitronectin (VN) was isolated and characterized from goat plasma in native and denatured state. Native VN consisted of 160 and >250 kDa polypeptides, whereas denatured VN showed bands of 81 and >250 kDa on SDS-gel. Storage of 81 kDa polypeptide for 3 days at 4 degrees C resulted in formation of 160 and >250 kDa proteins. Hence high molecular weight forms of VN may be dimer and multimeric forms of 81 kDa monomer. Both native as well as denatured VN showed cell adhesive activity. Cells bound to native VN were round, whereas cells adhered to denatured VN were fully spread, a characteristic also observed with 81 kDa polypeptide. The 81 kDa VN bound to Heparin, whereas the 160 kDa preparation did not bind to Heparin in presence of urea. Absence of EDTA resulted in the degradation of goat VN. Similarly, addition of excess Ca(2+) caused total degradation of VN polypeptides in buffers with EDTA, suggesting metalloprotease activity inthe protein.
Division of Biochemistry, Indian Veterinary Research Institute, Izatnagar (U.P.) 243 122, India.
S
S
Suchitra
Vasili
V
Ashok
Tapas
T
Gupta
Paritosh
P
Joshi
D000818:Animals; D002448:Cell Adhesion; D002522:Chlorocebus aethiops; D006041:Goats / Q000097:blood*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011489:Protein Denaturation; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D059748:Proteolysis; D012685:Sepharose / Q000031:analogs & derivatives / Q000737:chemistry; D014508:Urea / Q000737:chemistry; D014709:Vero Cells; D019096:Vitronectin / Q000097:blood / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*
D010446:Peptide Fragments; D019096:Vitronectin; C037405:heparin-sepharose; D014508:Urea; D012685:Sepharose