scholarly journals The Interaction(s) between Calf-Skin Hyaluronic Acid (Hyaluronan) and Dermal Type I Calf-Skin Collagen under 254 nm UV Radiation: Ability of Hyaluronan to Alter Qualitative and Quantitative Dimerization of Collagen Tyrosine Residues

2019 ◽  
Vol 09 (02) ◽  
pp. 51-59
Author(s):  
Julian M. Menter ◽  
La Toya Freeman ◽  
Ortega Edukye
Keyword(s):  
Hyaluronic Acid ◽  
Uv Radiation ◽  
Type I ◽  
Tyrosine Residues ◽  
Qualitative And Quantitative ◽  
Skin Collagen ◽  
Calf Skin

scholarly journals Completion of the amino acid sequence of the α1 chain from type I calf skin collagen. Amino acid sequence of α1(I)B8

1983 ◽  
Vol 215 (1) ◽  
pp. 183-189 ◽  
Author(s):  
R W Glanville ◽  
D Breitkreutz ◽  
M Meitinger ◽  
P P Fietzek
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Type I ◽  
Amino Acid Sequence Analysis ◽  
Complete Amino Acid Sequence ◽  
Skin Collagen ◽  
Arginine Residues ◽  
Calf Skin

The complete amino acid sequence of the 279-residue CNBr peptide CB8 from the alpha 1 chain of type I calf skin collagen is presented. It was determined by sequencing overlapping fragments of CB8 produced by Staphylococcus aureus V8 proteinase, trypsin, Endoproteinase Arg-C and hydroxylamine. Tryptic cleavages were also made specific for lysine by blocking arginine residues with cyclohexane-1,2-dione. This completes the amino acid sequence analysis of the 1054-residues-long alpha (I) chain of calf skin collagen.

scholarly journals Platelet-Collagen Interaction : Adhesion to Alpha 1 (I) CB6 and Alpha 1 (III) CB4 Peptides from Calf-Skin Collagen

1977 ◽  
Author(s):  
F. Fauvel ◽  
Y. J. Legrand ◽  
J. P. Caen
Keyword(s):  
Amino Acids ◽  
Platelet Adhesion ◽  
Type I Collagen ◽  
Blood Platelets ◽  
Type I ◽  
Adhesive Properties ◽  
Type Iii ◽  
Skin Collagen ◽  
Differential Filtration ◽  
Calf Skin

The interaction of blood platelets with collagen is the trigger of haemostasis and, at least partly, of thrombosis. Two types of fibrillar collagens (type I and type III), present in the vessel wall, can induce the adhesion of blood platelets. This study was designed to determine which part of their molecule is involved in that phenomenon. We then devised a quantitative test based upon differential filtration of non adhesive and adhesive 14c serotonin labeled platelets through a sepharose column for the evaluation of platelet adhesion to collagen or collagen derivatives. No differences were observed in the adhesive properties of calf-skin type I and type III collagens when the degree of multimerisation was identical. Isolated alpha 1 (I) and alpha 2 chains were not active ; but platelets adhered to reassociated (alpha .1 (I))3 trimers, not to (alpha 2)3 trimers ; in type I collagen, alpha 1 chains seems to have the most essential role for platelet adhesion. Various cyanogen bromide peptides were tested : only the 217 C-terminal amino acids alpha 1 CB6 from type I and the 149 central amino acids alpha 1 CB4 from type III were active.The adhesive properties of collagen seems then associated with chemical groupings localized in these peptides : a random folding of the entire isolated chains could make these “sites” unavailable to the platelets, whereas in the triple helix characteristic of fibrillar trimers, they would be more accessible. This could explain why fibrils and small peptides are active, while isolated chains are not.

PHOTOCHEMISTRY OF TYPE I ACID-SOLUBLE CALF SKIN COLLAGEN: DEPENDENCE ON EXCITATION WAVELENGTH

1995 ◽  
Vol 62 (3) ◽  
pp. 402-408 ◽  
Author(s):  
Julian M. Menter ◽  
George D. Williamson ◽  
Kimberly Carlyle ◽  
Cyril L. Moore ◽  
Isaac Willis
Keyword(s):  
Excitation Wavelength ◽  
Type I ◽  
Skin Collagen ◽  
Calf Skin

scholarly journals The effects of fixation by combination of glutaraldehyde/dimethyl suberimidate. Use of collagen as a model system.

1983 ◽  
Vol 31 (11) ◽  
pp. 1274-1278 ◽  
Author(s):  
M Tzaphlidou
Keyword(s):  
Fine Structure ◽  
Model System ◽  
Optical Data ◽  
Type I ◽  
Skin Collagen ◽  
Computer Aided ◽  
Dimethyl Suberimidate ◽  
Structural Preservation ◽  
Correlation Procedure ◽  
Calf Skin

The fixative behavior of glutaraldehyde/dimethyl suberimidate in combination was studied using reconstituted fibrils of type I calf skin collagen as a model system and comparing electron-optical data and chemical data by a computer-aided correlation procedure. The results confirm that the structural preservation of collagen obtained using prefixation in glutaraldehyde followed by dimethyl suberimidate fixation is less than when using dimethyl suberimidate and postfixation in glutaraldehyde. Furthermore, glutaraldehyde preserves the structure of collagen to a lesser degree than dimethyl suberimidate. With the combination of the two fixatives, the preservation of fine structure of collagen obtained is less than that when using dimethyl suberimidate alone.

Fluorescence of collagen - properties of tyrosine residues and another fluorescent element in calf skin collagen

FEBS Letters ◽  
1969 ◽  
Vol 5 (3) ◽  
pp. 187-191 ◽  
Author(s):  
Z. Deyl ◽  
R. Praus ◽  
H. Šulcová ◽  
J.N. Goldman
Keyword(s):  
Tyrosine Residues ◽  
Skin Collagen ◽  
Calf Skin

Thermal stability of calf skin collagen type I in salt solutions

1996 ◽  
Vol 1297 (2) ◽  
pp. 171-181 ◽  
Author(s):  
Regina Komsa-Penkova ◽  
Rumiana Koynova ◽  
Georgi Kostov ◽  
Boris G. Tenchov
Keyword(s):  
Thermal Stability ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Salt Solutions ◽  
Skin Collagen ◽  
Thermal Stability Of ◽  
Calf Skin

scholarly journals The Location of Cross-links in γ Chains from Calf Skin Collagen

1968 ◽  
Vol 243 (11) ◽  
pp. 2890-2898
Author(s):  
M P Drake ◽  
P F Davison
Keyword(s):  
Skin Collagen ◽  
Cross Links ◽  
Calf Skin

Assembly of Type I Collagen on PVA Film Induced by Glutaraldehyde Vapor

2011 ◽  
Vol 284-286 ◽  
pp. 1794-1799 ◽  
Author(s):  
Yu Lu Wang ◽  
Xue Pin Liao ◽  
Bi Shi
Keyword(s):  
Network Structure ◽  
Type I Collagen ◽  
Collagen Fibers ◽  
Type I ◽  
Collagen Concentration ◽  
Collagen Molecules ◽  
Induced Reaction ◽  
Calf Skin

Type I collagen was isolated from calf skin and its assembly on PVA film induced by glutaraldehyde vapor was investigated. It was found that the collagen molecules were firstly orientationally assembled into collagen fibers under the inducement of glutaraldehyde vapor. Then the collagen fibers could be further aggregated into novel network structure in proper conditions of the induced reaction. The morphology of the assembled collagen fibers was depended on induced time and concentration of collagen. The network arrangement could be obtained after being induced for 72h when collagen concentration was 2.5mg/ml. At higher concentration of collagen (5 mg/ml), the collagen fibers with larger dimension were obtained, but the growth of fibers was almost in one direction.

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