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Isolation and chemical characterization of collagen in bovine pulmonary tissues.

ABSTRACT: 1. The contents of the fibrous proteins collagen and elastin in the pleural and parenchymal regions of bovine lungs were determined. The collagen content was approx. 70% (g/100g of salt-extracted defatted powder) in each tissue, and the elastin content was 28% in pleura and 13.5% in parenchyma. 2. Purification of the insoluble collagen from the pleura and parenchyma of bovine lungs by various methods was attempted. The collagen fractions isolated after incubation of the pulmonary tissues with the proteolytic enzymes collagenase ("collagenase-soluble" fraction) or pancreatic elastase ("elastase-insoluble" fraction) each contained approx. 87% of the total collagen initially present. 3. Both collagen fractions were chemically analysed for their amino acid and carbohydrate contents and were found to be similar to those of the intact interstitial collagens isolated from skin, bone and tendon. 4. The contents of the two aldimine cross-linking compounds, dehydrohydroxylysinonorleucine and dehydrodihydroxylysinonorleucine, were determined in the bovine pulmonary collagen fractions, and were found to decrease with increasing age of the animals, and were similar to the values found in intact collagens from bone and tendon.

SUBMITTER: Francis G

PROVIDER: S-EPMC1165217 | biostudies-other | 1975 Feb

REPOSITORIES: biostudies-other

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Isolation from bovine elastic tissues of collagen type VI and characterization of its form in vivo.

Project description:Foetal-bovine nuchal ligament and aorta, together with adult-bovine aorta and pregnant uterus, were extracted under dissociative conditions in the absence and in the presence of a reducing agent. A collagenous glycoprotein of Mr 140000 [designated component 140K(VI)], identified in these extracts as the major periodate/Schiff-positive component, was shown to be related to collagen type VI. Digestion of non-reduced extracts with pepsin yielded periodate/Schiff-positive peptides that, on the basis of their electrophoretic mobilities, amino acid analyses and peptide 'maps', were identical with type VI collagen fragments prepared by standard procedures. It is concluded that collagen type VI occurs in vivo as molecule comprising three chains of Mr 140000 in which the helical domains account for about one-third of each polypeptide. Biosynthetic experiments with nuchal-ligament fibroblasts in culture demonstrated that a bacterial-collagenase-sensitive [3H]fucose-labelled glycoprotein, Mr 140000, was immunoprecipitated from culture medium by a specific antibody to the pepsin-derived form of collagen type VI. This result suggests that the collagenous polypeptides [140K(VI) components] represent the biosynthetic precursors of type VI collagen that do not undergo processing to smaller species before deposition in the extracellular matrix. Analyses of 5M-guanidinium chloride extracts of tissues with markedly different elastin contents and at different stages of development suggested that there was no relationship between collagen type VI and elastic-fibre microfibrils, a conclusion supported by the observation that the immunoprecipitated glycoprotein, Mr 140000, was distinct from the glycoprotein MFPI, Mr 150000, believed to be a constituent of these microfibrils [Sear, Grant & Jackson (1981) Biochem. J. 194, 587-598].

| S-EPMC1152638 | biostudies-other

Isolation and characterization of acidic structural glycoproteins in pulmonary tissues.

Project description:1. Extraction of the pleural and parenchymal regions of bovine lungs with salt and organic solvents gave powders that contained glycoproteins in addition to collagen and elastin. The contents of these glycoproteins (g/100 of powder) was 4% in pleura and 15.5% in parenchyma. 2. Attempts were made to purify these glycoproteins fromboth tissues by various methods. 3. Both tissues contained heterogeneous mixtures that were similar solubilities, had similar amino acid and carbohydrate compostions. 4. The compostions of the pulmonary glycoproteins resembled those isolated from other connective tissues by other workers.

| S-EPMC1165218 | biostudies-other

Time scale of glycation in collagen of bovine pericardium-derived bio-tissues.

Project description:Glycosyl-ation is the process of combining one or more glucose molecules (or other monosaccharides) with molecules of a different nature (which are therefore glycosyl-ated). In biochemistry, glycosyl-ation is catalyzed by several specific enzymes, and assumes considerable importance since it occurs mainly at the expense of proteins and phospho-lipids which are thus transformed into glycoproteins and glycolipids. Conversely, in diabetes and aging, glycation of proteins is a phenomenon of non-enzymatic nature and thus not easily controlled. Glycation of collagen distorts its structure, renders the extracellular matrix stiff and brittle and at the same time lowers the degradation susceptibility thereby preventing renewal. Based on models detailed in this paper and with parameters determined from experimental data, we describe the glycation of type 1 collagen in bovine pericardium derived bio-tissues, upon incubation in glucose and ribose. With arginine and lysine/hy-droxy-lysine amino acids as the primary sites of glycation and assuming that the topological polar surface area of the sugar molecules determines the glycation rates, we modelled the glycation as a function of time and determined the glycation rate and thus the progression of glycation as well as the resulting volume increase.

| S-EPMC8562672 | biostudies-literature

Isolation and characterization of cyanogen bromide peptides from the collagen of bovine articular cartilage.

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| S-EPMC1177750 | biostudies-other

Polyamine synthesis in mammalian tissues. Isolation and characterization of spermidine synthase from bovine brain.

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| S-EPMC1153573 | biostudies-other

Bovine aortic chondroitin sulphate- and dermatan sulphate-containing proteoglycans. Isolation, fractionation and chemical characterization.

Project description:1. Guanidinium chloride (4M) in the presence of proteinase inhibitors extracted 90% of bovine aorta galactosaminoglycans as proteoglycans that were subsequently purified by ion-exchange and gel chromatography. 2. Fractionation of the calcium salts of the purified proteoglycans with increasing concentration of ethanol yielded fractions PG-25 (28%), PG-35 (45%) and PG-50 (37%). 3. Fraction PG-50 contained proteochondroitin 6-sulphate, whereas fractions PG-25 and PG-35 were proteodermatan sulphates of greatly different carbohydrate composition; the molar proportions of L-iduronate-N-acetylgalactosamine 4-sulphate, D-glucuronate-N-acetyl-galactosamine 4-sulphate and D-glucuronate-N-acetylgalactosamine 6-sulphate were 75: 18 :7 in fraction PG-25 and 14 :46 :40 in fraction PG-35. 4. The presence of alternating or mixed sequences with L-iduronate- and D-glucuronate-containing repeating disaccharides was indicated by the formation of tetrasaccharides after chondroitinase AC digestion (single L-iduronate residues) and by the release of fragments containing four or five consecutive D-glucuronate-N-acetylgalactosamine repeats after periodate oxidation and alkaline elimination. 5. The amino acid compositions of fractions PG-25 and PG-35 were similar and markedly different from that of fraction PG-50, which also contained more side chains.

| S-EPMC1163122 | biostudies-other

The chemical composition of bovine vitreous-humour collagen fibres.

Project description:The insoluble protein fraction was prepared from the central and posterior peripheral fraction of bovine vitreous humour. The collagen present in this fraction was solubilized by pepsin and fractionated by gel chromatography. Analysis of the solubilized collagen fractions showed that the alpha-chain component had an amino acid composition and yielded a series of CNBr-cleavage peptides that showed it was very similar to type II collagen obtained from articular cartilage. Bovine vitreous-humour collagen alpha-chains differed, however, from those of cartilage collagen in that they had a lower alanine content and differed in their susceptibility to cleavage by CNBr. Satisfactory cleavage was obtained after two CNBr treatments involving reduction and alkylation. In addition, significant quantities of other peptides constituents were present in the vitreous-humour collagen fractions, and the galactose and glucose content of the alpha-chain fraction was more than double that of the same fraction obtained from articular cartilage. Although the origin of the additional peptide constituents in the vitreous-humour collagen preparations is not known, the results obtained indicate that they are probably not derived from a distinct type of alpha-chain component but may be terminal peptides covalently linked to the alpha 1 type-II helical portions of the collagen. The differences in the chemical composition of the vitreous-humour collagen indicate that vitreous-humour fibres are composed of a special type-II collagen.

| S-EPMC1161430 | biostudies-other

Isolation and molecular characterization of bovine enteroviruses in Egypt.

Project description:Enteroviruses belong to the Picornaviridae family and infect a wide range of mammals including cattle. Bovine enterovirus (BEV) has recently been reclassified into E and F serotypes. BEV was first isolated in Egypt in 1966 although it has been known in other countries since the 1950s. In this study, BEV-F2 was isolated from calves with severe diarrhea and the isolated viruses were subjected to molecular characterization. Illumina sequencing of one of the isolates revealed the presence of a complete BEV-F genome sequence. The phylogenetic analysis revealed nucleotide substitutions along the genome in comparison with other known strains of BEV-F (HQ663846, AY508697 and DQ092795). Two primer sets were designed from the 3D and 5'NTR regions and used for the examination of the remaining isolates, which were confirmed to be of the BEV-F2 serotype. The availability of the complete genome sequence of this virus adds to the sequence database of the members of Picornaviridae and should be useful in future molecular studies of BEV.

| S-EPMC7129267 | biostudies-literature

Expansion, isolation and first characterization of bovine Th17 lymphocytes.

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| S-EPMC6834651 | biostudies-literature

Bovine Ephemeral Fever in Iran: Diagnosis, Isolation and Molecular Characterization.

Project description:BACKGROUND:Bovine ephemeral fever (BEFV) is an arthropod-borne disease of cattle and water buffaloes. BEFV occurs seasonally in tropical, subtropical and temperate regions of Africa, Asia and Australia. It has been known for the past decades in Iran based on clinical signs but lack of an accurate diagnosis has made the real feature of disease obscured. This is the first scientific report on isolation and identification of the agent in which molecular diagnosis of BEFV was also set up with high sensitivity and specificity. METHODS:The viral agent was successfully isolated through serial passages in brain of suckling mice and cell culture. In addition, the circulating virus during the autumn 2012 in Iran was molecularly characterized based on partial G gene. RESULTS:Alignment of 3 virus sequences from different parts of Iran revealed that they are identical suggesting that the circulating viruses were most likely the same in this period. Phylogenetic analysis of the Iranian sequences with 17 sequences in the GenBank from the world showed that it is identical to the virus circulated in Turkey during the same period suggesting that the virus was circulated in a large geographic region. CONCLUSION:These results offer primary information about BEFV in Iran. To better understanding the epidemiology of the virus, further studies based on seroepidemiology, molecular epidemiology, entomology and meteorology together with finding the model of animal transportation in the region are necessary.

| S-EPMC4662791 | biostudies-literature

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