Thermitase from Thermoactinomyces vulgaris; amino acid sequence of the large N-terminal cyanogen bromide peptide

1985 ◽  
Vol 50 (4) ◽  
pp. 885-896 ◽  
Author(s):  
Bedřich Meloun ◽  
Miroslav Baudyš ◽  
Manfred Pavlík ◽  
Vladimír Kostka ◽  
Gert Hausdorf ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
High Performance ◽  
Cyanogen Bromide ◽  
Sequential Data ◽  
Amino Acid Residues ◽  
Methionine Residue ◽  
Large N ◽  
Thermoactinomyces Vulgaris

The large cyanogen bromide fragment (CB1) represents the N-terminal part of the molecule of thermitase and contains 226 amino acid residues. Its molecular weight calculated from sequential data is 22 932 (the C-terminal residue is regarded as a methionine residue in the calculations). The amino acid sequence of fragment CB1 was determined by analysis of peptides obtained by tryptic hydrolysis of the fragment; these data were complemented by sequence analysis of the chymotryptic digest of fragment Mf (residues 75 through 226) and of chymotryptic fragment ET3 (residues 103 through 226) isolated from the limited tryptic digest of fragment CB1. The peptides were purified by high performance liquid chromatography and by thin layer techniques. The sequence analysis of the large peptides was effected in the sequenator, small peptides were sequenced manually by the DABITC/PITC double coupling technique. The results obtained in this study together with those of previous work5 permitted the complete amino acid sequence of fragment CB1 to be determined.

Amino acid sequence of cyanogen bromide fragment CB5 of human hemopexin

1989 ◽  
Vol 54 (3) ◽  
pp. 803-810 ◽  
Author(s):  
Ivan Kluh ◽  
Ladislav Morávek ◽  
Manfred Pavlík
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acid Hydrolysis ◽  
Cyanogen Bromide ◽  
Polypeptide Chain ◽  
Amino Acid Residues ◽  
Mild Acid Hydrolysis ◽  
Methionine Residue ◽  
Cyanogen Bromide Fragment ◽  
Mild Acid

Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.

Amino acid sequence of the acidic acrosin inhibitor (BUSI I B2) from bull seminal plasma

1983 ◽  
Vol 48 (9) ◽  
pp. 2558-2568 ◽  
Author(s):  
Bedřich Meloun ◽  
Věra Jonáková ◽  
Dana Čechová
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Sequential Data ◽  
Amino Acid Residues

The molecule of the inhibitor consists of 63 amino acid residues whose sequence is the following: Glu-Ile-Tyr-Phe-Glu-Pro-Asp-Phe-Gly-Phe-Pro-Pro-Asp-Cys-Lys-Val-Tyr-Thr-Glu-Ala-Cys-Thr-Arg-Glu-Tyr-Asn-Pro-Ile-Cys-Asp-Ser-Ala-Ala-Lys-Thr-Tyr-Ser-Asn-Glu-Cys-Thr-Phe-Cys-Asn-Glu-Lys-Met-Asn-Asn-Asp-Ala-Asp-Ile-His-Phe-Gln-His-Phe-Gly-Glu-Cys-Glu-Tyr. The sequential data were obtained by the analysis of peptides isolated from the tryptic and chymotryptic digest of the carboxymethylated inhibitor. The molecular weight of the inhibitor calculated from its amino acid sequence is 7377.

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 Amino acid-sequence variability at the N-terminal extra piece of mouse immunoglobulin light-chain precursors of the same and different subgroups

1976 ◽  
Vol 157 (1) ◽  
pp. 145-151 ◽  
Author(s):  
Y Burstein ◽  
I Schechter
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Variable Region ◽  
Amino Acid Residues ◽  
Free System ◽  
Methionine Residue ◽  
N Terminus ◽  
Mouse Myeloma

The proteins programmed in the wheat-germ cell-free system by the mRNA coding for the MOPC-63 mouse myeloma L (light) chain were labelled with six radioactive amino acids: [35S]methionine, [4,5-3H]leucine, [3,4-3H]proline, [3-3H]serine, [4,5-3H]isoleucine or [2,3-3H]alanine. Amino acid-sequence analyses showed that over 90% of the total cell-free product was one homogeneous protein, which corresponds to the MOPC-63 L-chain precursor. In this precursor an extra piece, 20 amino acid residues in length, precedes the N-terminus of the mature L chain. The extra piece contains one methionine residue at the N-terminus, six leucine residues, which are clustered in two triplets at positions 6, 7, 8 and 11, 12, 13, one proline residue at position 16, and one serine residue at position 18. The closely gathered leucine residues, as well as their abundance (30%), suggest that the extra-piece moiety is hydrophobic. In the precursors, the extra piece is coupled to the variable region of the L chain. Partial sequences of precursors of L chains of the same and different subgroups that were labelled with the above six radioactive amino acids indicate that the extra piece is part of the variable region. Thus the precursors of MOPC-63 and MOPC-321 L chains, which are of the same subgroup, have extra pieces of identical size (20 residues), and so far their partial sequences are also identical (see above). On the other hand, in the precursor of MOPC-41 L chain, which is of a different subgroup, the extra piece is 22 residues in length. Further, the sequence of the MOPC-41 extra piece differs in at least ten positions from sequences of the extra pieces of the precursors of MOPC-63 and MOPC-321 L chains.

scholarly journals Isolation, properties and amino acid sequence of a long-chain neurotoxin, Acanthophis antarcticus b, from the venom of an Australian snake (the common death adder, Acanthophis antarcticus)

1981 ◽  
Vol 193 (3) ◽  
pp. 899-906 ◽  
Author(s):  
H S Kim ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intramuscular Injection ◽  
Amino Acid Residues ◽  
Methionine Residue ◽  
N Terminus ◽  
The Common ◽  
Ld50 Value ◽  
Almost All ◽  
Long Chain

The venom of an Australian elapid snake, the common death adder (Acanthophis antarcticus), was chromatographed on a CM-cellulose CM52 column. One of the neurotoxic components, Acanthophis antarcticus b (toxin Aa b) was isolated in about 9.4% (A280) yield. The complete amino acid sequence of toxin Aa b was elucidated. Toxin Aa b is composed of 73 amino acid residues, with ten half-cystine residues, and has a formula weight of 8135. Toxin Aa b has no histidine or methionine residue in its sequence. The amino acid sequence of toxin Aa b is homologous with those of other neurotoxins with known sequences, although it is novel in having a valine residue at its N-terminus and an arginine residue at position-23, where a lysine residue is found in almost all the so-far-known neurotoxins. Irrespective of the latter replacement, the toxin Aa b is fully active, with an LD50 value (in mice) of 0.13 microgram/g body weight on intramuscular injection.

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.

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