scholarly journals a-Chain Sequence of Newt Haemoglobin (Taricha granulosa)

1977 ◽  
Vol 30 (2) ◽  
pp. 1 ◽  
Author(s):  
MichaeI Coates ◽  
B Brimhall ◽  
Peter Stenzel ◽  
Mark Hermodson ◽  
David Gibson ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Taricha Granulosa ◽  
N Terminus ◽  
Lysine Residues ◽  
Arginine Residues ◽  
Chain Sequence ◽  
Methionine Residues ◽  
A Chain

The amino acid sequence of the IX-chain of the major haemoglobin of a newt, T. granulosa, has been determined. The chain is 142 residues long and has an extra methionine at its N-terminus when compared with human IX-chain. Most of the tryptic peptides were sequenced by a combination of the subtractive Edman method and by deduction from the compositions of overlapping fragments produced by various enzymic treatments. The sequence of two 'core' regions was obtained by automatic sequencing of large peptides produced by trypsin cleavage at arginine residues only after blockage of lysine residues by citraconylation; by cleavage between aspartic acid and proline residues with 70% formic acid, and by cyanogen bromide cleavage at methionine residues.

Amino acid sequence of cyanogen bromide fragments CB4 and CB6 of hog pepsin

1981 ◽  
Vol 46 (3) ◽  
pp. 626-639
Author(s):  
Ladislav Morávek
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Disulfide Bond ◽  
Sequential Analysis ◽  
Cyanogen Bromide ◽  
Serine Residue ◽  
Aspartic Acid Residue ◽  
N Terminus ◽  
Methionine Residues ◽  
Cyanogen Bromide Fragment

By the analyses of chymotryptic, and thermolytic peptides the amino acid sequence was determined of cyanogen bromide fragment CB4 representing the region of the pepsin chain between the N-terminus and methonine-residue I: Ile-Gly-Asp-Glu-Pro-Leu-Glu-Asn-Tyr-Leu-Asp-Thr-Glu-Tyr-Phe-Gly-Thr-Ile-Gly-Ile-Gly-Thr-Pro-Ala-Gln-Asp-Phe-Thr-Val-Ile-Phe-Asp-Thr-Gly-Ser-Ser-Asn-Leu-Trp-Val-Pro-Ser-Val-Tyr-Cys-Ser-Ser-Leu-Ala-Cys-Ser-Asp-His-Asn- + Gln-Phe-Asn-Pro-Asp-Asp-Ser-Ser-Thr-Phe-Glu-Ala-Thr-Ser-Gln-Glu-Leu-Ser-Ile-Thr-Tyr-Gly- + Thr-Gly-Ser-Met. The serine residue (Ser) in position 68 of pepsin is phosphorylated. By sequential analysis of chymotryptic, tryptic, and thermolytic peptides the amino acid sequence was determined of cyanogen bromide fragment CB6 representing the region between methionine residues II and III in the pepsin chain: Asp-Gly-Glu-Thr-Ile-Ala-Cys-Ser-Gly-Gly-Cys-Gln-Ala- + Ile-Val-Asp-Thr-Gly-Thr-Ser-Leu-Leu-Thr-Gly-Pro-Thr-Ser-Ala-Ile-Ala-Asn-Ile-Gln-Ser-Asp- + Ile-Gly-Ala-Ser-Glu-Asn-Ser-Asp-Gly-Glu-Met. The aspartic acid residue (Asp) in position 16 of this fragment is identical with the residue reacting with diazo inhibitors which forms a part of the active center of the enzyme. Both half-cystine residues of fragment CB4 and fragment CB6 are linked to one another by a disulfide bond in native pepsin.

Amino acid sequence of cyanogen bromide fragment CB3 of hog pepsin

1981 ◽  
Vol 46 (3) ◽  
pp. 655-666
Author(s):  
Ladislav Morávek ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Methionine Residues ◽  
Cyanogen Bromide Fragment

On the basis of the knowlidge of thermolytic, chymotryptic and substilisin peptides the amino acid sequence was determined of cyanogen bromide fragment CB3 representing the region between methionine residues I and II of pepsin: Thr-Gly-Ile-Leu-Gly-Tyr-Asp-Thr-Val-Gln-Val-Gly-Gly-Ile-Ser-Asp-Thr-Asn-Gln-Ile-Phe-Gly-Leu-Ser-Glu-Thr-Glu-Pro-Gly-Ser-Phe-Leu-Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu-Gly-Leu-Ala-Tyr-Pro-Ser-Ile-Ser-Ala-Ser-Gly-Ala-Thr-Pro-Val-Phe-Asp-Asn-Leu-Trp-Asp-Gln-Gly-Leu-Val-Ser-Gln-Asp-Leu-Phe-Ser-Val-Tyr-Leu-Ser-Ser-Asn-Asp-Asp-Ser-Gly-Ser-Val-Val-Leu-Leu-Gly-Gly-Ile-Asp-Ser-Ser-Tyr-Tyr-Thr-Gly-Ser-Leu-Asn-Trp-Val-Pro-Val-Ser-Val-Glu-Gly-Tyr-Trp-Gln-Ile-Thr-Leu-Asp-Ser-Ile-Thr-Met.

scholarly journals Haemoglobins of the Shark, Heterodontus Portusjacksoni II. Amino Acid Sequence of the a-Chain

1976 ◽  
Vol 29 (2) ◽  
pp. 73 ◽  
Author(s):  
AR Nash ◽  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Paper Chromatography ◽  
Cyanogen Bromide ◽  
Gel Filtration ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Amino Terminal ◽  
Core Peptide ◽  
A Chain

The amino acid sequence of the a-chain of the principal haemoglobin from the shark, H. portusjacksoni has been determined. The chain has 148 residues and is acetylated at the amino terminal. The soluble peptides obtained by tryptic and chymotryptic digestion of the protein or its cyanogen bromide fragments were isolated by gel filtration, paper ionophoresis and paper chromatography. The amino acid sequences were determined by the dansyl-Edman procedure. The insoluble 'core' peptide from the tryptic digestion contained 34 residues and required cleavage by several proteases before the sequence was established. Compared with human a-chain there are 88 amino acid differences including the additional seven residues which appear on the amino terminal of the shark chain. There is also one deletion and one insertion. The chain contains no tryptophan but has four cysteinyl residues which is the highest number of such residues recorded for a vertebrate globin.

scholarly journals Partial amino acid sequence of rat pre-prolactin

1977 ◽  
Vol 161 (1) ◽  
pp. 189-192 ◽  
Author(s):  
R A Maurer ◽  
J Gorski ◽  
D J McKean
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Cysteine Residue ◽  
Amino Acid Residues ◽  
Partial Amino Acid Sequence ◽  
Considerable Similarity ◽  
Rat Pituitary ◽  
N Terminus ◽  
Methionine Residues

Rat pituitary mRNA was used to direct the cell-free synthesis of pre-prolactin labelled with [4,5-3H]leucine and either [35S] methioninc or [35S] cystine. Sequence analysis of the labelled protein indicates that pre-prolactin has 29 amino acid residues joined to the N-terminus of the prolactin sequence. Leucine residues were found at positions 13, 14, 15, 16, 21 and 22, methionine residues at positions 1, 17 and 18, and a cysteine residue at position 24 of the precursor sequence, and this partial sequence shows considerable similarity with other precursors that have been sequenced.

scholarly journals The amino acid sequence of troponin I from rabbit skeletal muscle

1975 ◽  
Vol 149 (2) ◽  
pp. 493-496 ◽  
Author(s):  
J M Wilkinson ◽  
R J A. Grand
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Troponin I ◽  
Rabbit Skeletal Muscle ◽  
British Library ◽  
Amino Acid Residues ◽  
N Terminus

The complete amino acid sequence of rabbit skeletal muscle troponin I was determined by the isolation of the cyanogen bromide fragments and the tryptic methionine-containing peptides. Troponin I contains 179 amino acid residues and has a molecular weight of 20864. Its N-terminus is acetylated. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50055 (23 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.

scholarly journals Amino Acid Sequence Studies on Sheep Liver Fructose-bisphosphatase. II The Complete Sequence

1983 ◽  
Vol 36 (3) ◽  
pp. 235 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Fructose Bisphosphatase ◽  
Proteolytic Digestion ◽  
Sheep Liver ◽  
Methionine Residues

The cyanogen bromide fragments of S-carboxymethylated fructose-bisphosphatase were purified. The amino acid sequences of the small fragments were determined by the dansyl-Edman method. The large fragments were subjected to proteolytic digestion to give smaller peptides more amenable for purification and sequencing by similar methods. Enzyme digests of the S-carboxymethylated enzyme gave overlap peptides containing the methionine residues.

Peptide vaccine against canine parvovirus: identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence.

1995 ◽  
Vol 69 (11) ◽  
pp. 7274-7277 ◽  
Author(s):  
J I Casal ◽  
J P Langeveld ◽  
E Cortés ◽  
W W Schaaper ◽  
E van Dijk ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Vaccine ◽  
Canine Parvovirus ◽  
N Terminus
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