scholarly journals Chymotryptic and tryptic peptides of fragment α1-CB3 from bovine corneal collagen. Pinpointing the sites of hexose attachment

1978 ◽  
Vol 171 (3) ◽  
pp. 697-703 ◽  
Author(s):  
N A Panjwani ◽  
J J Harding
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Collagen Fibres ◽  
Tryptic Peptides ◽  
Amino Acid Compositions ◽  
Skin Collagen ◽  
Calf Skin ◽  
Corneal Collagen ◽  
Overlap Region

Tryptic peptides of citraconylated fragment alpha1-CB3 and chymotryptic peptides of fragment alpha1-CB3 of bovine corneal collagen were prepared, isolated and characterized. Their amino acid compositions were consistent with the amino acid sequence of fragment alpha1-CB3 from calf skin collagen. Two glycoside sites were identified in bovine corneal fragment alpha1-CB3, one of them being the first located in the overlap region of collagen. The results are related to the uniformly narrow collagen fibres found in cornea and essential for its transparency.

scholarly journals Completion of the amino acid sequence of the α1 chain from type I calf skin collagen. Amino acid sequence of α1(I)B8

1983 ◽  
Vol 215 (1) ◽  
pp. 183-189 ◽  
Author(s):  
R W Glanville ◽  
D Breitkreutz ◽  
M Meitinger ◽  
P P Fietzek
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Type I ◽  
Amino Acid Sequence Analysis ◽  
Complete Amino Acid Sequence ◽  
Skin Collagen ◽  
Arginine Residues ◽  
Calf Skin

The complete amino acid sequence of the 279-residue CNBr peptide CB8 from the alpha 1 chain of type I calf skin collagen is presented. It was determined by sequencing overlapping fragments of CB8 produced by Staphylococcus aureus V8 proteinase, trypsin, Endoproteinase Arg-C and hydroxylamine. Tryptic cleavages were also made specific for lysine by blocking arginine residues with cyclohexane-1,2-dione. This completes the amino acid sequence analysis of the 1054-residues-long alpha (I) chain of calf skin collagen.

The covalent structure of collagen: Amino acid sequence of α1-CB3 from calf skin collagen

FEBS Letters ◽  
1972 ◽  
Vol 26 (1-2) ◽  
pp. 74-76 ◽  
Author(s):  
Peter P. Fietzek ◽  
Peter Wendt ◽  
Ingrid Kell ◽  
Klaus Kühn
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Skin Collagen ◽  
Covalent Structure ◽  
Calf Skin

scholarly journals The amino acid sequence of the carboxyterminal nonhelical cross link region of the α 1 chain of calf skin collagen

FEBS Letters ◽  
1972 ◽  
Vol 21 (1) ◽  
pp. 75-79 ◽  
Author(s):  
J. Rauterberg ◽  
P. Fietzek ◽  
F. Rexrodt ◽  
U. Becker ◽  
M. Stark ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cross Link ◽  
Skin Collagen ◽  
Calf Skin

scholarly journals The Covalent Structure of Collagen. 2. The Amino-Acid Sequence of alpha1-CB7 from Calf-Skin Collagen

1973 ◽  
Vol 38 (2) ◽  
pp. 396-400 ◽  
Author(s):  
Peter P. Fietzek ◽  
Friedrich W. Rexrodt ◽  
Kelvin E. Hopper ◽  
Klaus Kuhn
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Skin Collagen ◽  
Covalent Structure ◽  
Calf Skin

scholarly journals Studies on the subunit structure and amino acid sequence of triose phosphate isomerase from chicken breast muscle

1974 ◽  
Vol 139 (1) ◽  
pp. 11-22 ◽  
Author(s):  
Anna J. Furth ◽  
J. D. Milman ◽  
J. D. Priddle ◽  
R. E. Offord
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Triose Phosphate Isomerase ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Rabbit Muscle ◽  
Tryptic Peptides ◽  
Amino Acid Compositions ◽  
Triose Phosphate

1. Triose phosphate isomerase was prepared by chromatography on DEAE-cellulose of an (NH4)2SO4 fraction of an extract of homogenized chicken breast muscle. The product is homogeneous on gel electrophoresis and is suitable for growing crystals for X-ray work. The specific activity is 10000 units/mg and the value for E0.1%280 is 1.20. 2. Comparison between the sum of the amino acid compositions of the tryptic peptides of the protein and the amino acid composition obtained on total hydrolysis of the protein indicates that the relative subunit mass is about 27000. 3. These data, together with the results of the examination of the amino acid compositions of a number of minor peptides, the number of peptides in the tryptic digest and the complete amino acid sequences of the tryptic peptides (the determination of which is described here), give no indication that the subunits are dissimilar. 4. A tentative amino acid sequence is presented for the protein, in which the ordering of the tryptic peptides is derived by homology with the sequence of the rabbit muscle enzyme (Corran & Waley, 1973). 5. An appendix describes the use that was made of mass spectrometry in the determination of some of the sequences. Mass-spectrometric data have been obtained for 35 residues, that is about 15% of the total sequence of the protein. 6. An extended version of the present paper has been deposited as Supplementary Publication SUP 50025 at the British Library, Lending Division (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1973) 131, 5.

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