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.

Structure of a Plasmodium yoelii gene-encoded protein homologous to the Ca(2+)-ATPase of rabbit skeletal muscle sarcoplasmic reticulum

1990 ◽  
Vol 97 (3) ◽  
pp. 487-495
Author(s):  
K. Murakami ◽  
K. Tanabe ◽  
S. Takada
Keyword(s):  
Skeletal Muscle ◽  
Plasma Membrane ◽  
Amino Acid ◽  
Sarcoplasmic Reticulum ◽  
Amino Acid Sequence ◽  
Plasmodium Yoelii ◽  
Transmembrane Domains ◽  
Rabbit Skeletal Muscle ◽  
Parasite Development ◽  
Amino Acid Residues

A cation-transporting ATPase gene of Plasmodium yoelii was cloned from the parasite genomic library using an oligonucleotide probe derived from a conserved amino acid sequence of the phosphorylation domain of the aspartyl phosphate family of ATPases. The complete nucleotide sequence was determined and it predicts a 126,717 Mr encoded protein composed of 1115 amino acids. Northern blot analysis revealed that the gene is transcribed during the asexual stages of parasite development. The P. yoelii protein contains functional and structural features common to the family of aspartyl phosphate cation-transporting ATPases. The parasite protein shows the highest overall homology in amino acid sequence (42%) to the Ca2(+)-ATPase of rabbit skeletal muscle sarcoplasmic reticulum. Homologies to other aspartyl phosphate cation-transporting ATPases including a plasma membrane Ca2(+)-ATPase were between 13 and 24%. The structure predicted from a hydropathy plot also shows 10 transmembrane domains, the number and location of which correlated well with the sarcoplasmic reticulum Ca2(+)-ATPase. On the basis of these results, we conclude that the parasite gene encodes an organellar, but not plasma membrane, Ca2(+)-ATPase. The P. yoelii protein, furthermore, contains all six amino acid residues in the transmembrane domains that were recently identified as comprising a high-affinity Ca2(+)-binding site. It follows that organellar Ca2(+)-ATPases of rabbit and Plasmodium conserve functionally important amino acid residues, even though they are remote from each other phylogenetically.

scholarly journals The amino acid sequence of a carbohydrate-containing fragment of hen ovotransferrin.

1975 ◽  
Vol 147 (3) ◽  
pp. 463-472 ◽  
Author(s):  
I B Kingston ◽  
J Williams
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
British Library ◽  
Single Chain ◽  
N Terminus

1. Hen ovotransferrin was treated with CNBr and fractionated by gel filtration. 2. After further treatment by reduction and carboxymethylation a carbohydrate-containing fragment of molecular weight 11990 was obtained (fragment BCd). 3. The amino acid sequence of this fragment was determined. It consists of a single chain of 94 residues. 4. The structure of a tryptic glycopeptide derived from whole ovotransferrin permitted a further eight residues to be assigned at the N-terminus of fragment BCd. 5. Heterogeneity was found at two positions. 6. Further evidence has been deposited as Supplementary Publication SUP 50045 (19 pages) at the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1975), 145, 5.

scholarly journals The amino acid sequence of rabbit slow-muscle troponin I.

1977 ◽  
Vol 167 (1) ◽  
pp. 183-192 ◽  
Author(s):  
Roger J. A. Grand ◽  
J. Michael Wilkinson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Troponin I ◽  
Proteolytic Enzymes ◽  
Vastus Lateralis ◽  
Slow Muscle ◽  
British Library ◽  
Blocking Group ◽  
Single Polypeptide Chain ◽  
N Terminus

Troponin I was isolated from six red muscles in the hind leg of the rabbit. Soleus, semi-tendinosus, vastus intermedius and adductor longus muscles contained primarily slow-muscle troponin I, vastus lateralis contained fast-muscle troponin I and quadratus femoris contained a mixture of the two. The complete amino acid sequence of the troponin I from slow muscle was determined. Seven CNBr fragments were isolated and sequenced by using the dansyl–Edman technique after digestion with proteolytic enzymes. The CNBr fragments were ordered by isolation of tryptic peptides containing carboxy[14C]methyl-methionine. Direct evidence for the conjunction of residues 8 and 9 has not been obtained, and one of the carboxyl groups between residues 71 and 79 may carry an amide group. Slow-muscle troponin I is a single polypeptide chain of 184 residues with a mol.wt. of 21146. It has a net overall positive charge of 18 at pH7, and an absorption coefficient, A1%,1cm280, of 5.43. The protein was isolated with both a blocked and an unblocked N-terminus, although the nature of the blocking group was not determined. Proline was found to be the N-terminal amino acid. Two forms of the protein could also be distinguished by the presence of an extra two residues at the C-terminus. Comparison of sequences of troponin I from rabbit slow, fast and cardiac muscle shows that homology is most marked in the C-terminal half of the molecules. Towards the N-terminus the homology becomes much less marked. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50079 (32 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained in the terms given in Biochem. J. (1977), 161, 1.

scholarly journals Studies on Marsupial Proteins IV. Amino Acid Sequence of Myoglobin From the Red Kangaroo, Megaleia Rufa

1971 ◽  
Vol 24 (1) ◽  
pp. 75 ◽  
Author(s):  
GM Air ◽  
EOP Thompson
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Amino Acid Sequences ◽  
Single Component ◽  
Amino Acid Residues ◽  
Histidine Residues ◽  
Complete Amino Acid Sequence ◽  
Red Kangaroo

Myoglobin isolated from skeletal muscle of M. rufa consists of a single component containing 153 amino acid residues. The complete amino acid sequence has been determined. Oleavage with cyanogen bromide gave four polypeptides which were further fragmented by digestion with trypsin or chymotrypsin. The amino acid sequences of the peptides obtained were determined by the "dansyl"-Edman procedure. The order of the cyanogen bromide fragments was readily deduced from terminal sequences. Digestion of maleylated myoglobin with trypsin and cleavage at histidine residues with N-bromosuccinimide gave some overlapping sequences. Amino acid sequences in myoglobins are more conservative than in the ,B-chains of haemoglobin previously studied (Air and Thompson 1969) but the red kangaroo myoglobin shows more variation in amino acid sequence than has been found in myoglobins from other species.

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 Acylphosphatase from Rabbit Skeletal Muscle

1985 ◽  
Vol 97 (4) ◽  
pp. 1155-1161 ◽  
Author(s):  
Takako KIZAKI ◽  
Toshihide TAKASAWA ◽  
Yusuke MIZUNO ◽  
Hiroyuki SHIOKAWA
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rabbit Skeletal Muscle
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