EFFECTS OF INVITRO N-GLUCOSYLATION ON TYPE-I COLLAGEN FIBRILLOGENESIS
EFFECTS OF INVITRO N-GLUCOSYLATION ON TYPE-I COLLAGEN FIBRILLOGENESIS
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DOI：
10.1007/bf01114964
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发表时间：
1981-01-01
影响因子：
4
通讯作者：
MUH, JP
中科院分区：
文献类型：
--
作者：
GUITTON, JD;LEPAPE, A;MUH, JP
在体外将来自大鼠尾腱的酸溶性胶原糖基化，并首先在35 ℃下测定原纤维形成参数。C，然后在4.degree。C.增加的滞后期和半衰期与非酶结合葡萄糖的量有关，这可能是由于在纤维形成的早期阶段疏水相互作用减少。分子间交联的不存在和在4 ° C下纤维的部分再溶解。通过比浊法和EM研究，C表明葡萄糖基化胶原纤维的成熟过程中存在缺陷。
Acid-soluble collagen from rat tail tendon was glucosylated in vitro and fibrillogenesis parameters were determined first at 35.degree. C then at 4.degree. C. Increased lag phase and half time were related to the amount of non-enzymatically bound glucose, probably due to a decrease of hydrophobic interactions at this early stage of fibril formation. The absence of intermolecular cross-links and the partial redissolution of fibrils at 4.degree. C, as investigated both by turbidimetry and EM, suggests a defect in the maturation process in glucosylated collagen fibrils.