Biomedical subjects
J E Finch
Publications and source records attributed to J E Finch.
The covalent structure of cartilage collagen. Amino acid sequence of residues 552-661 of bovine alpha1(II) chains.
The covalent structure of the first 111 residues from the N-terminus of peptide alpha1(II)-CB10 from bovine nasal-cartilage collagen is presented. This region comprises residues 552-661 of the alpha1(II) chain. The sequence was determined by automated Edman degradation of peptide alpha1(II)-CB10 and of peptides produced by cleavage with trypsin and hydroxylamine. Comparison of this region of the alpha1(II) chain with the homologous segment of the alpha1(I) chain indicated a homology level of 85%, slightly higher than that of 81% reported for the N-terminal region of the alpha1(II) chain (Butler, Miller & Finch (1976) Biochemistry15, 3000-3006). The occurrence of two residues of glycosylated hydroxylysine was established at positions 564 and 603, the first present exclusively as galactosylhydroxylysine and the latter as a mixture of galactosylhydroxylysine and glucosylgalactosylhydroxylysine. Also, two residues at positions 648 and 657 were tentatively identified as glycosylated hydroxylysines. The amino acid sequences adjacent to the hydroxylysine residues so far identified in the alpha1(II) chain were compared with the homologous regions of the alpha1(I) and alpha2 chains, but no obvious prerequisite for hydroxylation could be seen. From comparison with the homologous sequence of the alpha1(I) chain, it appears that the alpha1(II)-chain sequence presented here contains three more amino acids than that reported for the alpha1(I) chain. This triplet would be interposed between residues 63 and 64 of the reported sequence of peptide alpha1(I)-CB7 from calf skin collagen. Data on the purification of the subpeptides and their amino acid compositions have been deposited as Supplementary Publication SUP 50087 (7 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.
A bacteriological survey of the domestic environment.
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Effect of growth environment on Pseudomonas aeruginosa killing by rabbit polymorphonuclear leudocytes and cationic proteins.
Pseudomonas aeruginosa grown in a chemostat under carbon- and magnesium-limited conditions showed varying resistance to killing by rabbit peritoneal exudate polymorphonuclear leukocytes. Slow-growing (D = 0.05 h-1), magnesium-limited cells were significantly more resistant to the lethal effects of the phagocytes than were fast-growing magnesium-limited cells and carbon-limited cells (D = 0.05 h-1 and D = 0.5 h-1, respectively). The resistance of magnesium-limited cells to killing by cationic proteins isolated from the leukocytes was shown to be growth-rate dependent, the slowest-growing (D = 0.05 h-1) cells being the most resistant. Carbon-limited cells were sensitive to killing by the cationic proteins at all growth rates tested. Antisera raised in rabbits to all types of cells and commercial anti-Pseudomonas serum rapidly agglutinated magnesium-limited cells but failed to agglutinate carbon-limited cells. There was some indication that slow-growing (D = 0.05 h-1), magnesium-limited cells agglutinated most readily with both types of antisera. No difference was detected in the mouse toxicity of heat-killed cells grown under the various conditions.
Covalent structure of cartilage collagen. Amino acid sequence of residues 363-551 of bovine alpha1(II) chains.
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The covalent structure of cartilage collagen. Evidence for sequence heterogeneity of bovine alpha1(II) chains.
During studies on the amino acid sequence of bovine nasal cartilage collagen, the cyanogen bromide peptide alpha1(II)-CB11 was degraded to smaller peptides with trypsin. One of the tryptic peptides, T5, which contained 39 residues was shown by amino acid and sequence analyses to occur in a predominant form that contained glutamine at position 5 and in a second form with leucine at this site. In addition to the heterogeneity at this position, amino acid analyses of five different preparations revealed that the peptide with leucine contained a seryl residue not found in the major form. Sequence heterogeneity at a third position of alpha1(II) was demonstrated by the isolation of a hexapeptide (T2) from the trypsin digest of alpha1(II)-CB11 which contained 0.21 residue of alanine and 0.77 of leucine. Both the leucine and alanine of T2 were removed after the second cycle of subtractive Edman degradation. These data show that at least two types of alpha1(II) chains, designated as alpha1(II)Major and alpha1(II)Minor, exist in bovine nasal cartilage. Further considerations suggest that these two chains are probably not variants derived from allelic genes but are the products of separate genes.
The covalent structure of cartilage collagen. Amino acid sequence of the NH2-terminal helical portion of the alpha 1 (II) chain.
The amino acid sequence of 162 residues from the NH2-terminal region of bovine alpha 1 (II) is reported. Automated sequence analysis of chains from pepsin-treated type II collagen indicated the sequence and order of two CNBr peptides, alpha 1 (II)-CB2 and alpha 1 (II)-CB3, at the beginning of the repetitive triplet sequence of alpha 1 (II). The sequences of alpha 1 (II)-CB6, alpha 1 (II),-CB12, and 39 residues of alpha 1 (II)-CB11 were determined largely by automated Edman degradation. Comparative sequence data are reported which indicate that the level of homology between alpha 1 (I) and alpha 1 (II) chains in the NH2-terminal region is about 80%. A similar level of homology was reported for the central portions of these chains (Butler, W.T., Miller, E.J., Finch, J.E., Jr., and Inagami, T. (1974), Biochem. Biophys. Res. Commun. 57 190). The degree of intraspecies variability between chain types is thus greater than the interspecies variability for a single chain type. Within the sequence reported here, the alpha 1 (II) chain contains glucosylgalactosylhydroxylysine at three positions. The corresponding sequence of alpha 1 (I) contains only one clycosylated hydroxylysine with the other two positions occupied by lysyl residues.
Cleavage of Type II and III collagens with mammalian collagenase: site of cleavage and primary structure at the NH2-terminal portion of the smaller fragment released from both collagens.
Collagenase cleavage of human Type II and III collagens has been studied using a highly purified preparation of rabbit tumor collagenase. Progress of the reactions in solution was followed by viscometry and the results indicated that under the conditions employed Type III collagen molecules were cleaved at approximately five times the rate of Type II molecules. Cleavage products of the reactions were isolated in denatured form by agarose molecular sieve chromatography. The molecular weights and amino acid compositions of the products demonstrated that Type II and III molecules had been cleaved at the characteristic three-quarter, one-quarter locus, giving rise to a large fragment derived from the NH2-terminal portion of the molecule and a smaller fragment representing the COOH-terminal region. The amino acid sequence at the NH2-terminal portion of the smaller fragment derived from Type II collagen was determined to be Ile-Ala-Gly-Gln-Arg, and the corresponding region from Type III collagen was found to have the sequence Leu-Ala Gly-Leu-Arg. These sequences for alpha1(II) and alpha1(III) chains adjacent to the site of collagenase cleavage along with previous data for alpha1(I) and alpha2 chains indicate that the minimum specific sequence required for collagenase cleavage is Gly-Ile-Ala or Gly-Leu-Ala. Inspection of the available sequence data for collagen alpha chains indicates that the latter sequences are found in at least three additional locations at which collagenase cleavage does not occur. Each of the sequences which are apparently not substrates for collagenase, however, are followed by a Gly-X-Hyp sequence. We suggest, then, that a minimum of five residues in collagen alpha chains COOH-terminal to the cleavage site comprise the substrate recognition site.
Specific cleavage of the native type III collagen molecule with trypsin. Similarity of the cleavage products to collagenase-produced fragments and primary structure at the cleavage site.
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The influence of nutrient limitation in a chemostat on the sensitivity of Pseudomonas aeruginosa to polymyxin and to EDTA.
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Chemical studies on the cyanogen bromide peptides of rat skin collagen. Amino acid sequence of alpha 1-CB3.
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Homologous regions of collagen alpha1(I) and alpha1(II) chains: apparent clustering of variable and invariant amino acid residues.
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Chemical character of proteins in rat incisors.
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The sensitivity of urinary pathogens seen in a private pathological practice.
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