IDENTIFICATION OF THE NONCOLLAGENOUS PROTEINS OF BOVINE BONE BY TWO-DIMENSIONAL GEL-ELECTROPHORESIS
IDENTIFICATION OF THE NONCOLLAGENOUS PROTEINS OF BOVINE BONE BY TWO-DIMENSIONAL GEL-ELECTROPHORESIS
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DOI:
10.1007/bf02405335
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发表时间:
1984-01-01
影响因子:
4.2
通讯作者:
MANN, KG
中科院分区:
文献类型:
--
作者:
DELMAS, PD;TRACY, RP;MANN, KG
The noncollagenous proteins of bovine bone were characterized using 2 high-resolution gel electrophoretic techniques. Proteins were extracted from bone tissue by extended dialysis against 0.5 M EDTA. In some cases, a preextraction was done in guanidine HCl. Bovine plasma was also examined to identify the proteins in bone that might also be present in blood. Major, reproducible spots (160) were scored on a standard preparation bone map. These comprise about 40 individual protein groups. There are many more minor spots present which puts the total number present over 200. Of these groups, 15 are not present on plasma maps. Bone proteins identified in this way include actin, bone Gla-protein and osteonectin. The remainder are unknown. Bone Gla-protein is present in bovine bone in 4 isoelectric forms, pI [isoelectric point] = 3.95-4.50. Electroblotting analysis of EDTA and guanidine HCl extracted material failed to reveal any higher MW immunologically reactive species. The plasma proteins found in bone include, but are not limited to albumin, apo A-I lipoprotein, IgG, IgM, transferrin, .alpha.-2-HS-glycoprotein and Hb. Extraction with guanidine HCl plus EDTA significantly enriches the yield for the nonplasma proteins but does not appear to extract any additional bone proteins.