Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cyanogen bromide peptides were prepared from insoluble bovine skin and dentin collagens and compared by electrophoresis in polyacrylamide gels containing sodium dodecylsulphate, with those of the alpha1 and alpha2 chains of soluble type I and type III collagen. Both insoluble collagens yielded predominantly the peptides of type I collagen. Insoluble skin collagen was approximately 13% type III. Type III collagen if present in dentin, is present in smaller quanitity not detected by the technique used here. Several new fragments, different in each tissue, were obtained which could not be accounted for as uncleaved peptides. Three of those from dentin were isolated by gel chromatography and characterized by amino acid analysis. Two were found to contain 3-hydroxyproline, suggesting the presence of alpha1CB6. The recovery of only 25-30% of alpha1CB6 in the expected position on SDS gel electrophoresis indicated that it was involved in interactions with other peptides in these two tissues to the extent of one and a half cross-links per tropocollagen molecule. The nature and distributin of cross-link peptides of bovine skin and dentin collagens was distinctly different.
 ...
PMID:The cyanogen bromide peptides of bovine soluble and insoluble collagens. II. Tissue specific cross-linked peptides of insoluble skin and dentin collagen. 13 73

The uptake of latex by fibroblasts in confluent primary culture results in the secretion of collagenase at a linear rate for a prolonged period. Phagocytosis might therefore constitute an important level of collagenase regulation in corneal ulceration. The collagenase in cell cultures is present in a latent form (40,000 MW) like that obtained from organ cultures of ulcerating corneas and can be activated proteolytically. Production of the latent collagenase in cell culture depends upon the presence of serum and diminishes greatly when serum is removed from the medium. Collagenase activity can be demonstrated after the latent collagenase has been separated from serum antiproteases in the media. Alternatively, careful titration of the crude media with trypsin to saturate serum antiproteases, to release collagenase from the complex with alpha 2-macroglobulin, and to activate latent collagenase also results in measurable collagenase activity. The collagenase that is secreted cleaves fibrillar type I collagen and cleaves soluble type I collagen into the typical 3/4 and 1/4 length fragments, as demonstrated by SDS-gel electrophoresis and electron microscopy.
 ...
PMID:Collagenase from corneal cell cultures and its modulation by phagocytosis. 22 35

A method for the separation of type III collagen from type I collagen by SDS-polyacrylamide gel electrophoresis has been developed. This is based on the observation that the presence of 3-4 M urea decreases the mobility of the alpha 1 [III] chain to a greater extent than those of the alpha 1[I] and alpha 2 chains, although the alpha 1[I] and alpha 1[III] chains move at the same rate in the absence of urea. An attempt to separate the alpha 1[II] chain of type II collagen from the alpha 1[I] chain was unsuccessful under the experimental conditions employed.
 ...
PMID:Separation of the alpha chains of type I and III collagens by SDS-polyacrylamide gel electrophoresis. 47 38

The cyanogen bromide peptides from insoluble and pepsin solubilised type I collagen of bovine bone, dentine, meniscus, tendon, skin and cornea were compared by SDS-polyacrylamide gel electrophoresis. In each case alpha 1CB6 was shown to be the only peptide of molecular weight greater than 10 000 involved in cross-linking. The major helical peptides alpha 1CB3, alpha 1CB8, alpha 1CB7 and alpha 2CB4 were not implicated in cross-linking in any tissue either by end overlap or helix-helix interaction. The C-terminal alpha 2 chain peptide alpha 2CB3,5, which contains a large helical region, was not involved in cross-linking to any large peptides, although a slight increase in molecular weight in all tissues examined did suggest a possible interaction(s) with a very small peptide of molecular weight 4--5000.
 ...
PMID:Bovine type I collagen: A study of cross-linking in various mature tissues. 50 99

For the first time, it has been possible to solubilize a significant amount of heart valve collagen from 6 month old pigs by pepsin treatment. Chromatographic and electrophoretic analysis of this pepsin-soluble collagen gives evidence for the presence of two types of collagen molecules: type I collagen and another type which has properties similar to those of type III collagen. For example, this collagen, present as a gamma component, gives rise, when reduced by dithiothreitol, to two bands by SDS-acrylamide gel electrophoresis: a beta band and an alpha band. Furthermore, the collagenic web of this tissue is highly polymerized, which explains the inability to solubilize all of the collagen molecules and the presence of high-molecular-weight molecules in the pepsin-soluble fractions.
 ...
PMID:Collagen heterogeneity in pig heart valves. 77 39

Human nucleus pulposus and annulus fibrosus, obtained at autopsy from patients 7-30 years of age, were extracted with 2 M guanidine-HCl (pH 5.82) to remove proteoglycans, then stirred with pepsin in 0.5 M acetic acid, followed by three 24-h extractions with 1 M NaCl (pH 7.5) and one 24-h extraction with 2 M KSCN (potassium thiocyanate) (pH 7.2). Pepsin and NaCl solubilized an average of about 30% of nucleus pulposus collagen and 18% of annulus fibrosus collagen. KSCN extracted a further 34% of nucleus pulposus collagen and only 4% of annulus fibrosus collagen. CM-cellulose chromatography of nucleus and annulus collagen purified from the pepsin, NaCl and KSCN supernatants consistently revealed only one peak, always appearing slightly ahead of the alpha1 position for rat tail tendon type I collagen. Polyacrylamide and SDS-gel electrophoresis consistently revealed only one band with the mobility of alpha1 chains. Amino acid composition of collagen from nucleus and annulus is comparable to those of mammalian and avian cartilage type II collagen, and distinctly different from those of rat tail tendonand guinea pig skin type I collagens. Periodate oxidation of nucleus and annulus collagens showed that 81% and 67%, respectively, of the hydroxylysine residues survive treatment, compared to 71% for bovine articular cartilage collagen and 17% for guinea pig skin collagen. Total hexose analysis revealed 1.8 muM and 2.0 muM hexose per muM periodate-stable hydroxylysine in nucleus and annulus collagens, respectively. Ion exchange chromatography showed the presence of glucose and galactose in a ratio of 0.92:1 in nucleas collagen and 1.07:1 in annulus collagen. Pepsin-solubilized, NaCl-extracted collagen from nucleus and annulus formed native-type fibrils in vitro. The banding patterns of ATP-induced segment-long-spacing precipitates of nucleus and annulus collagens were identical to each other and indistinguishable from those of cartilage (type II) collagen, but distinctly different from those of rat tail tendon (type I) collagen. These data suggest that the collagen which can be extracted after limited pepsin attack of human nucleus and annulus is of the form [alpha1 (II)]3.
 ...
PMID:Pepsin-solubilized collagen of human nucleus pulposus and annulus fibrosus. 78 25

Undecalcified frozen sections, 40 mu thick, were cut from the knee articular cartilage of young adult Baboons (Papio papio). The sections were freeze dried and the superficial and the intermediate zones were separated by microdissection under a binocular dissecting microscope. The material of each zone was cleaved with CNBr and the major peptides were analyzed by discelectrophoresis in SDS polyacrylamide. Peptides alpha, CB 3,5 and alpha, (II) CB 10 were used as characteristic markers for type I and type II collagen respectively. The method could detect as little as 5-10% of type I collagen of total collagen in mixtures. The thin superficial zone contains type I and type II collagen. The intermediate zone contains only type II collagen. The possible biological significance of this different anatomical distribution of the two types of collagen is discussed. This special distribution could explain the contradictory data from the literature concerning the presence of type I collagen in the articular cartilage.
 ...
PMID:[Differences in distribution of type I and type II collagens in the superficial and intermediary zones of articular cartilage]. 82 75

Procollagen and collagen were isolated from the culture medium and cell layer of line TSD4 (obtained from mouse teratocarcinoma OTT6050). SDS-polyacrylamide gel electrophoresis of the highly purified procollagen fraction demonstrated that the fraction is composed of theta chains (150,000 daltons), pro alpha chains (130,000 daltons), and alpha chains (100,000 daltons). Limited pepsin digestion of this fraction yielded a single species of collagen molecules having a chain composition (alpha1)3, as did collagen isolated from the cell layer. Each alpha1 chain appears to be slightly larger than alpha1 chains from calf or human type I and type III collagen. Amino acid analysis and cyanogen bromide peptide profiles of pepsin-treated TSD4 collagen demonstrated significant differences from those of other collagens (II, III, IV) of the type alpha1(X)3, although similar to that of the alpha1 chain of type I collagen, [alpha1(1)]2alpha2. Taken together, acrylamide gel electrophoresis, amino acid composition, electron microscopy, and cyanogen bromide peptide analysis indicate that this material represents a new molecular species of collagen not previously characterized, probably related to [alpha1(I)]3.
 ...
PMID:Procollagen and collagen produced by a teratocarcinoma-derived cell line, TSD4: evidence for a new molecular form of collagen. 83 50

In 48 h incubation L-929 (L-5) cells secreted collagenous protein accounting for 16% of the total protein. CM-chromatography, SDS-acrylamide gel electrophoresis and DEAE-cellulose chromatography revealed that the collagenous protein was mainly composed of type I collagen, having no collagen of type III. In addition, precursor-form collagen and tropocollagen molecules were found to be present in the incubate.
 ...
PMID:Characterization of the synthesized collagen by mouse L-929 (L-5) cells. 93 37

The alpha chains and the major CNBr - derived peptides of collagen of growth cartilage were studied in the following syndromes: thanatophoric dwarfism, pseudothanatophoric dwarfism, achondroplasia, pseudoachondroplasia, diastrophic dwarfism, metatropic dwarfism, Kniest disease, parastremmatic dwarfism, multiple exostoses, Blount disease and pycnodysostosis. After extraction of proteoglycans the collagen was solubilized by limited pepsin digestion purified, and the alpha chains were analysed by electrophoresis. The major CNBr - derived peptides were obtained by cleaving directly the cartilage after proteoglycan extraction. In some syndromes purified collagen was also cleaved. The CNBr peptides were analyzed by disc electrophoresis in SDS-polyacrylamide. Human normal growth cartilage and baboon cartilage were used as controls. The pattern of alpha chains and of major CNBr peptides was similar in all the cases studied, except one case of lethal diastrophic dwarfism in which the pattern of peptides showed the presence of type I collagen in quantities detectable by the present method. However in a milder case of diastrophic dwarfism the pattern of CNBr peptides was found normal. The present study does not exclude possible abnormalities of collagen at a higher lever of supramolecular organization in osteochondrodysplasias.
 ...
PMID:[Study by gel electrophoresis, of alpha chains and of CNBr peptides of collagen from epiphyseal cartilage in chondrodysplasia]. 108


1 2 3 4 5 6 7 8 9 10 Next >>