Purification of bovine urinary beta2-microglobulin and its biochemical characteristics.
In this study, bovine beta2-m was purified from urine by ion-exchange chromatography and gel chromatography, and the characteristics were compared with those of colostral beta2-m by the immunological reactivity, isoelectric points, peptide map, and amino acid sequence. The characteristics of purified urinary beta2-m were consistent with those of the colostral beta2-m. The urinary and colostral beta2-m possessed the same polypeptide chain consisting of 98 amino acids, and its molecular weight is 11.8 kDa. Furthermore, four isoforms of beta2-m were found. The isoelectric points were different from each other.
Hoshi
F
F
Laboratory of Veterinary Internal Medicine, School of Veterinary Medicine and Animal Science, Kitasato University, Towada, Aomori, Japan.
Nagai
D
D
Nakajima
Y
Y
Higuchi
S
S
Kawamura
S
S
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel / Q000662:veterinary; D002851:Chromatography, High Pressure Liquid / Q000662:veterinary; D002852:Chromatography, Ion Exchange / Q000662:veterinary; D003126:Colostrum / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel / Q000662:veterinary; D005260:Female; D007526:Isoelectric Point; D008969:Molecular Sequence Data; D010449:Peptide Mapping / Q000662:veterinary; D001613:beta 2-Microglobulin / Q000652:urine*
D001613:beta 2-Microglobulin