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Type III procollagen and collagen in skin

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
A form of collagen, containing three alpha chains of type III, can be extracted from foetal calf, calf and rat skin under physiological conditions. This native collagen was purified by DEAE-cellulose chromatography and then was analysed by polyacrylamide gel electrophoresis which showed it consisted of several high molecular weight components, the size
A, Lenaers, C M, Lapiere
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Type III collagen in the intervertebral disc

The Histochemical Journal, 1991
Several collagen types have now been isolated from the intervertebral disc, although type III collagen has previously only been extracted from human pathological disc. In this study, type III collagen has been isolated from normal human and bovine intervertebral disc and immunolocalized in sections of rat, sheep, bovine and 'normal' human ...
S, Roberts   +3 more
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Type III collagen and probably not type I collagen aggregates platelets

Thrombosis Research, 1976
Abstract Type I collagen and type III collagen were extracted from foetal calf skin and used for inducing platelets aggregation in vitro . When added under its soluble form, type III collagen was found to be a faster and a most powerful platelet aggregating factor.
J, Hugues   +3 more
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Collagen Type III Glomerulopathies

Advances in Chronic Kidney Disease, 2012
The 2 rare disorders characterized by the pathological accumulation of collagen type III in glomeruli are discussed. These are collagenofibrotic glomerulopathy, also known as collagen type III glomerulopathy, and the nail-patella syndrome. Although there are similarities in abnormal morphology, with type III collagen in mesangium and/or capillary walls,
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Type I and Type III Collagens in Cutaneous Mucinosis

The American Journal of Dermatopathology, 1998
Cutaneous mucinoses are a heterogeneous group of diseases characterized by the focal or diffuse dermal deposition of glycosaminoglycans. The histopathologic examination of many cutaneous mucinoses reveals that the collagen fibers are fragmented. We wanted to characterize the type I (COL1) and type III (COL3) collagen distribution in skin biopsy ...
M F, Alves   +3 more
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The presence of type III collagen in the developing tooth

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1978
Type I and type III collagens have been isolated from dental papilla and dental pulp of bovine tissues by enzymic digestion with pepsin and differential salt precipitation. Type III collagen was further purified by molecular sieve and ion-exchange chromatography.
C A, Shuttleworth   +2 more
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Crosslinking in type III collagen of fetal tissue

Biochemical and Biophysical Research Communications, 1978
Abstract Native bovine amnion tissue was reduced with NaB 3 H 4 and type III collagen was isolated by pepsin digestion. Examination of the crosslink content of type III collagen following acid hydrolysis revealed the presence of dihydroxy- and hydroxylysinonorleucine in a ratio of 9 to 1.
D J, Cannon, P F, Davison
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Covalent binding of acetaldehyde to type III collagen

Biochemical and Biophysical Research Communications, 1989
Incubation of neutral salt soluble type III pN-collagen with [14C]acetaldehyde in vitro resulted in the formation of spontaneously stable acetaldehyde-protein adducts. This reaction occurred primarily at lysine residues and it was not affected by 0.2-2 mM concentrations of ascorbate but addition of sodiumcyanoborohydride increased the stable adducts by
A, Jukkola, O, Niemelä
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Conformational selection and collagenolysis in Type III collagen

Proteins: Structure, Function, and Bioinformatics, 2009
AbstractMatrix metalloproteases (MMPs) cleave native collagen at a single site despite the fact that collagen contains more than one scissile bond that can, in principle, be cleaved. For peptide bond hydrolysis to occur at one specific site, MMPs must (1) localize to a region near the unique scissile bond, (2) bind residues at the catalytic site that ...
Ramon, Salsas-Escat, Collin M, Stultz
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Studies on the sulfhydryl groups in type III collagen

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1976
The Type III collagen molecule, [alpha](III)]3, is comprised of three alphal(III) chains each of which contains two cysteinyl residues. Free sulfhydryl groups, however, could not be detected in the denatured, trimeric gamma-component of Type III collagen as judged by the failure to form derivatives with the alkylating reagents iodo-[14C]acetic acid and
M, Schneir, E J, Miller
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