ชื่อเรื่อง | : | Molecular loci and glycosylation of dehydro-histidinohydroxymerodesmosine in non-mineralized type I collagen fibrils |
นักวิจัย | : | Sirivimol Srisawasdi |
คำค้น | : | Collegen Type I , Cross-Linking Reagents , Dehydro-histidinohydroxymerodesmosine |
หน่วยงาน | : | จุฬาลงกรณ์มหาวิทยาลัย |
ผู้ร่วมงาน | : | Prasit Pavasant , Mitsuo, Yamauchi , Chulalongkorn University. Faculty of Dentistry |
ปีพิมพ์ | : | 2543 |
อ้างอิง | : | 9741306016 , http://cuir.car.chula.ac.th/handle/123456789/5813 |
ที่มา | : | - |
ความเชี่ยวชาญ | : | - |
ความสัมพันธ์ | : | - |
ขอบเขตของเนื้อหา | : | - |
บทคัดย่อ/คำอธิบาย | : | Thesis (Ph.D.)--Chulalongkorn University, 2000 The covalent intermolecular cross-linking is essential in providing collagen matrices with physicochemical properties. Dehydro-histidinohydroxymerodesmosine is a major tetravalent collagen cross-link present in most non-mineralized tissues. Despite its abundance, this cross-link has been poorly characterized. The objectives of this study were to isolate the cross-linked peptides, determine the molecular loci and evaluate the state of glycosylation of the cross-link. The peripheral layer of the turkey leg tendon (never-mineralized collagenous tissue) was reduced with tritiated sodium borohydride, subjected to sequential enzymatic/chemical digestion and several cross-linked peptides were isolated by means of HPLC. Based on the amino-terminal sequence, amino acid composition and mass spectrometric analyses of the purified peptides, three molecular loci were identified. They are lysyl aldehyde (alpha1-9N) X lysyl aldehyde (alpha1-9N) X hydroxylysine (alpha1-930) X histidine (alpha2-935), lysyl aldehyde (alpha1-9N) X lysyl aldehyde (alpha2-6N) X hydroxylysine (alpha1-930) X histidine (alpha2-935) and lysyl aldehyde (alpha1-9N) X lysyl aldehyde (alpha2-6N) X hydroxylysine (alpha1-930) X histidine (alpha1-932). The data indicate that the aldol involved in the cross-link is derived from the amino-terminal telopeptidyl aldehydes, and that the hydroxylysine on an alpha1 chain (residue 930) and histidine from alpha2-935 is the preferred cross-linking site. The latter suggests a stereospecific packing of the type I collagen molecules in the fibril. In addition, chemical and mass spectroscopic analyses of the peptides and their acid/base hydrolysates revealed that the hydroxylysine residues (alpha1-930) that are involved in the formation of this complex cross-link were not glycosylated. These results suggest that the carbohydrate moiety on the alpha1-930 hydroxylysine may have a role in regulating the cross-link formation. |
บรรณานุกรม | : |
Sirivimol Srisawasdi . (2543). Molecular loci and glycosylation of dehydro-histidinohydroxymerodesmosine in non-mineralized type I collagen fibrils.
กรุงเทพมหานคร : จุฬาลงกรณ์มหาวิทยาลัย. Sirivimol Srisawasdi . 2543. "Molecular loci and glycosylation of dehydro-histidinohydroxymerodesmosine in non-mineralized type I collagen fibrils".
กรุงเทพมหานคร : จุฬาลงกรณ์มหาวิทยาลัย. Sirivimol Srisawasdi . "Molecular loci and glycosylation of dehydro-histidinohydroxymerodesmosine in non-mineralized type I collagen fibrils."
กรุงเทพมหานคร : จุฬาลงกรณ์มหาวิทยาลัย, 2543. Print. Sirivimol Srisawasdi . Molecular loci and glycosylation of dehydro-histidinohydroxymerodesmosine in non-mineralized type I collagen fibrils. กรุงเทพมหานคร : จุฬาลงกรณ์มหาวิทยาลัย; 2543.
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