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牛牙龈胶原酶:证明与初步特性研究

Bovine gingival collagenase: demonstration and initial characterization.

作者信息

Birkedal-Hansen H, Cobb C M, Taylor R E, Fullmer H M

出版信息

J Oral Pathol. 1974;3(5):232-8. doi: 10.1111/j.1600-0714.1974.tb01716.x.

DOI:10.1111/j.1600-0714.1974.tb01716.x
PMID:4376818
Abstract

A collagenase active against native collagen was found in culture fluids of bovine gingiva. The enzyme first appeared in the culture fluid after 1-2 days and could be harvested thereafter for at least 30 days. The collagenase attacked collagen fibrils and cleaved collagen in solution, resulting in reaction products 1/4 and 3/4 of the length of the original molecule. The enzyme was inhibited by serum, by EDTA and by cysteine. The molecular weight was estimated by gel filtration to be 63,000 daltons.

摘要

在牛牙龈的培养液中发现了一种对天然胶原蛋白有活性的胶原酶。该酶在培养1-2天后首次出现在培养液中,此后至少30天可进行收获。这种胶原酶能攻击胶原纤维并裂解溶液中的胶原蛋白,产生的反应产物长度为原始分子的1/4和3/4。该酶受到血清、乙二胺四乙酸(EDTA)和半胱氨酸的抑制。通过凝胶过滤法估计其分子量为63,000道尔顿。

相似文献

1
Bovine gingival collagenase: demonstration and initial characterization.牛牙龈胶原酶:证明与初步特性研究
J Oral Pathol. 1974;3(5):232-8. doi: 10.1111/j.1600-0714.1974.tb01716.x.
2
Initial characterization of a neutral metalloproteinase, active on native 3/4-collagen fragments, synthesized by ROS 17/2.8 osteoblastic cells, periodontal fibroblasts, and identified in gingival crevicular fluid.对一种中性金属蛋白酶的初步特性研究,该酶对天然3/4型胶原片段有活性,由ROS 17/2.8成骨细胞、牙周成纤维细胞合成,并在龈沟液中被鉴定出来。
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Some characteristics of collagenase activity in gingival crevicular fluid and its relationship to gingival diseases in humans.龈沟液中胶原酶活性的一些特征及其与人类牙龈疾病的关系。
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Nature of collagenolytic enzyme and inhibitor activities in crevicular fluid from healthy and inflamed periodontal tissues of beagle dogs.
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Characterization and serum inhibition of neutral collagenase from cultured dog gingival tissue.培养犬牙龈组织中性胶原酶的特性及血清抑制作用
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Collagen breakdown by gingival collagenase and elastase.牙龈胶原酶和弹性蛋白酶导致的胶原蛋白分解。
Experientia. 1980 Apr 15;36(4):395-6. doi: 10.1007/BF01975107.

引用本文的文献

1
Pathology of collagen degradation. A review.胶原蛋白降解的病理学。综述。
Am J Pathol. 1978 Aug;92(2):508-66.