Covalent structure of collagen. Amino acid sequence of α1-CB6A of chick skin collagen

Sn, Dixit; Jm, Seyer; Ao, Oronsky; Corbett, Clare; Ah, Kang; Gross, Jerome

doi:10.1021/bi00680a020

Cited by 24 publications

(13 citation statements)

References 21 publications

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“…Since these regions represent sites of interchain cross-link formation, such treatment can be used to aid in extraction of insoluble collagen from tissues. Pepsin Dixit et al (1975b) Fietzek and Rexrodt (1975) Fietzek and Rexrodt (1975) Fietzek and Rexrodt (1975) α Residues in the helical region of collagen are numbered as in Table IX. treatment has been particularly effective in solubilization of types II and III collagen (see Section II,B,2).…”

Section: B Fragments Resulting From Limited Enzymatic Digestionmentioning

confidence: 99%

“…Cleavage at Asn-Gly bonds with hydroxylamine has proved useful in sequence determinations of several large BrCN fragments including rat «1-CB3 (Butler et al, 1974), rat «1-CB8 (Balian et al, 1971, chick «1-CB6A (Dixit et al, 1975b), and bovine «2-CB4 (Fietzek and Rexrodt, 1975) (see Table VIII). Extensive nonspecificity of the reaction, suggested by the findings of Deselnicu et al (1973) with the bovine a2 chain, was not encountered by Fietzek and Rexrodt (1975) in analyses of «2-CB4.…”

Section: Hydroxylamine Fragmentsmentioning

confidence: 99%

See 1 more Smart Citation

The Chemistry and Biology of Collagen

Börnstein¹,

Traub²

1979

The Proteins

183

119

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Section: B Fragments Resulting From Limited Enzymatic Digestionmentioning

confidence: 99%

Section: Hydroxylamine Fragmentsmentioning

confidence: 99%

The Chemistry and Biology of Collagen

Börnstein¹,

Traub²

1979

The Proteins

183

119

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“…The Slow Peptide-DMAA (07 1472) program of Beckman Instruments was employed. Small peptides were treated with 2-amino-1,5-naphthalenedisulfonic acid in the presence of Nethyl-"-[3-(dimethylamino)propyl]carbodiimide to help retain the peptides in the reaction cup (Foster et al, 1973;Dixit et al, 1975). The phenylthiohydantoin amino acids were identified either by high-pressure liquid chromatography (Zimmerman et al, 1973) or after hydrolysis to their parent amino acids (Smithies et al, 1971).…”

Section: Resultsmentioning

confidence: 99%

Covalent structure of collagen: amino acid sequence of .alpha.1(III)-CB9 from type III collagen of human liver

Seyer¹,

Kang²

1981

Biochemistry

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The peptide alpha 1(III)-CB9 was prepared and purified from human liver, and its amino acid sequence was determined. Automated Edman degradation of the intact peptide and peptides derived from selective cleavage with hydroxylamine and digestions with trypsin, thermolysin, and Staph V8 protease enabled determination of the complete amino acid sequence. The peptide alpha 1(III)-CB9 represents the COOH terminus of the helical (pepsin-resistant) portion of type III collagen and terminates in a Cys-Cys sequence responsible for the intramolecular disulfide cross-linkages with other chains. The present work completes the entire amino acid sequence of the helical (pepsin-resistant) portion of human cirrhotic liver type III collagen consisting of peptides alpha 1-(III)-CB3-7-6-1-8-10-2-4-5-9. The COOH terminus of human liver alpha 1(III) contained two additional triplets which, together with the extra triplet at the NH2 terminus in alpha 1(III)-CB3, make the helical portion of type III collagen longer than alpha 1(I) by nine residues (three Gly-X-Y triplets). The helical region of human liver type III collagen, therefore, consists of 1023 amino acids or 341 triplets.

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“…The protein-Quadrol (10 mM) program (122974) of Beckman Instruments was used (18). The phenylthiohydantoin-amino acids were identified by high-pressure liquid chromatography (19).…”

mentioning

confidence: 99%

Repeating covalent structure of streptococcal M protein.

Beachey¹,

Seyer²,

Kang³

1978

Proc. Natl. Acad. Sci. U.S.A.

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We have attempted to identify the covalent structure of the M protein molecue of group A streptococci that is responsible for inducing type-specific, protective immunity. M protein was extracted from type 24 streptococci, purified, and cleaved with cyanogen bromide. Seven cyanogen bromide peptides were purified and further characterized. Together, the peptides account for the entire amino acid content of the M protein molecule. Each of the purified peptides possessed the type-specific determinant that inhibits opsonic antibodies for group A streptococci. The primary structures of the aminoterminal regions of each of the purified peptides was studied by automated Edman degradation. The partial sequences of two of the peptides were found to be identical to each other and to that ofthe uncleaved M protein molecule through at least the first 27 residues. The amino-terminal sequences of the remaining five peptides were identical to each other through the twentieth residue but completely different from the aminoterminal region of the other two peptides. However, the typespecific immunoreactivity and the incomplete analysis of the primary structure of the seven peptides suggest that the antiphagocytic determinant resides in a repeating amino acid sequence in the M protein molecule. The opsonic and presumably protective antibodies against group A streptococci are directed exclusively against the type-specific M protein antigen located on the surface of virulent organisms. Attempts to immunize humans against streptococcal infections have been hampered by toxic reactions to vaccines prepared from almost any streptococcal product, including various M protein preparations (1). Crossreactive toxic moieties are often closely associated with the M protein molecule; the conventional methods of extraction and purification have failed to consistently separate the M protein from these moieties, which account for toxic reactions in the skin (2-5) and in the blood (6, 7).Several years ago Cunningham and Beachey (8) showed that limited peptic digestion abolished the toxic properties while retaining type-specific immunogenicity of purified preparations of M protein. Subsequently, M protein was extracted directly from group A streptococci by subjecting the intact organisms to limited digestion with pepsin (9). The peptic extracts of M protein (pep M) were then purified to homogeneity, and the antigen was readily separable from crossreactive toxic materials (10). In its purified form the M antigen was immunogenic in laboratory animals, producing high titers of typespecific opsonic antibodies without producing crossreactive antibodies against M-associated antigens (10, 11). Furthermore, the purified antigen was well tolerated in skin tests of guinea pigs and humans (11,12).Having obtained satisfactory yields of purified pep M protein, we thought it of interest to study the primary structure ofThe costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marke...

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Covalent structure of collagen. Amino acid sequence of α1-CB6A of chick skin collagen

Cited by 24 publications

References 21 publications

The Chemistry and Biology of Collagen

The Chemistry and Biology of Collagen

Covalent structure of collagen: amino acid sequence of .alpha.1(III)-CB9 from type III collagen of human liver

Repeating covalent structure of streptococcal M protein.

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