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Bovine skin

Extensive analysis of cyanogen bromide fragmented peptides of type I, III, and V collagens by MALDI-MS has shown that type V collagen from bovine skin is highly glycosylated, while type I and III collagens contain... [Pg.499]

Volpin, D., Veis, A. Isolation and characterization of the cyanogen-bromide peptides from the al and a2 chains of acid-soluble bovine skin collagen. Biochemistry 10, 1751 (1971)... [Pg.126]

The use of chemiluminescence technique has expanded to others natural polymers. Recently, Millington et al. reported studies on polymers such as the fibrous proteins wool and feather keratin, silk fibroin, and reconstituted collagen from bovine skin, which revealed new information about their degradation [81]. The potential of CL to analyze the effectiveness of treatments to protect the polymer during processing could contribute to diminish the loss of properties of the types of polymers widely used in textile industry. [Pg.114]

S. Sassa, S. Schwartz, G. Ruth (1981). Accumulation of protoporphyrin IX from 5-aminolevulinic acid in bovine skin fibroblasts with hereditary erythropoietic protoporphyria. A gene-dosage effect. J. Exp. Med., 153, 1094-1101. [Pg.98]

No electron density corresponding to residues 1-21 was observed in the crystal structure of the protein core of bovine skin decorin (21). These residues are therefore disordered and presumably serve as a flexible tether for the attachment of the single DS chain. [Pg.159]

Chopra RK, Pearson CH, Pringle GA, Fackre DS, Scott PG. Dermatan sulphate is located on serine-4 of bovine skin proteodermatan sulphate. Demonstration that most molecules possess only one glycosaminoglycan chain and comparison of amino acid sequences around glycosylation sites in different proteoglycans. Biochem J 1985 232 277-279. [Pg.171]

Scott PG, Dodd CM. The A-linked oligosaccharides of bovine skin proteo-dermatan sulphate. Biochem Soc Trans 1989 17 1031-1032. [Pg.172]

Scott PG, Dodd CM. Self-aggregation of bovine skin proteodermatan sulphate promoted by removal of the three A-linked oligosaccharides. Connect Tissue Res 1990 24 225-235. [Pg.172]

Zangrando D, Gupta R, Jamieson AM, Blackwell J, Scott PG. Light scattering studies of bovine skin proteodermatan sulfate. Biopolymers 1989 28 1295-1308. [Pg.174]

DH Lloyd. Evaluation of a cup scrub technique for quantification of the microbial flora on bovine skin. J Appl Bacteriol 56(1) 103-107, 1984. [Pg.392]

Takaoka, K., Koezuka, M., and Nakahara, H., 1991, Telopeptide-depleted bovine skin collagen as a carrier for bone morphogenetic protein, J. Orthop. Res. 9 902-907. [Pg.44]

The major sources of collagen I for in vitro applications are rat tail tendons, bovine Achilles tendons, and bovine skin. The extraction procedure requires partial solubiUzation of the collagen molecules under acidic conditions and may involve a treatment with pepsin to remove telopeptides and thereby decrease immunogenicity (Mano, 2013). Yet, the latter step may disturb the subsequent self-assembly of the molecules into fibrils (fibrillogenesis) and is therefore not always performed. Of note, collagen II can also be obtained from articular cartilages, but the complexity... [Pg.38]

Mozersky, S. M. Wildermuth, R. J. Manner, W. N. Estimation of the sulfated glycosaminoglycan content of bovine skin with Alcian blue. J. Am. Leather Chem. Assoc. 2003, 98, 337-343. [Pg.9]

Bacillus subtilis P6 Keratinase Bovine skin Giongo et al. (2007)... [Pg.227]

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