Physical and immunochemical properties of low-buoyant-density proteoglycans from avian cartilage.
Physical and immunochemical properties of low-buoyant-density proteoglycans from avian cartilage.
复制标题
禽类软骨低浮力密度蛋白多糖的物理和免疫化学特性。
DOI:
10.1016/0003-9861(81)90361-1
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发表时间:
1981
影响因子:
3.9
通讯作者:
Goetinck,PF
中科院分区:
文献类型:
--
作者:
McKeown-Longo,PJ;Sparks,KJ;Goetinck,PF
A proteoglycan link fraction (A1D5) from avian xyphoid cartilage contains one link protein and low-buoyant-density proteoglycans. An antiserum made against this fraction (anti-A1D5serum) specifically binds [35S]sulfate-labeled proteoglycans from aggregate (A1), monomer (A1D1), and link (A1D5) fractions synthesized by 14-day embryonic chick sterna. When [35S]sulfate-labeled proteoglycans from either monomer (A1D1) or link (A1D5) fractions are used as the antigen, anti-A1D5serum binds as well as an antiserum against a purified monomer preparation (anti-A1D11400 Vo serum). However, reduction and alkylation of the proteoglycans from the monomer fraction does reveal differences in the binding of the two antisera. Whereas reduction and alkylation of the antigen (35S-A1D1) inhibit binding by both antisera, binding of the anti-A1D5serum is more affected by antigen alteration. Differences in the two antisera can also be detected in assays using labeled aggregate as antigen. Anti-A1D5serum cannot maintain the same levels of antigen binding as the anti-A1D1-1400 Vo serum when compared in an antibody dilution curve. In addition, anti-A1D1-1400 Vo serum can stabilize aggregate during sedimentation in a sucrose density gradient containing 4mguanidine hydrochloride whereas anti-A1D5serum cannot. These results suggest that the low-buoyant-density proteoglycans found in the link (A1D5) fraction from avian cartilage contain some of the antigenic determinants found on the proteoglycan monomer. However, there is at least one monomer determinant which is not present in the A1D5fraction.