scholarly journals The amino acid sequence of rabbit skeletal muscle troponin C: Gene replication and homology with calcium -binding proteins from carp and hake muscle

FEBS Letters ◽  
1973 ◽  
Vol 36 (3) ◽  
pp. 268-272 ◽  
Author(s):  
John H. Collins ◽  
James D. Potter ◽  
Marcus J. Horn ◽  
Gedelita Wilshire ◽  
Nora Jackman
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Troponin C ◽  
Calcium Binding Proteins ◽  
Rabbit Skeletal Muscle ◽  
Gene Replication

scholarly journals Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family

1999 ◽  
Vol 338 (3) ◽  
pp. 583-589 ◽  
Author(s):  
Tsuyoshi SHISHIBORI ◽  
Yuhta OYAMA ◽  
Osamu MATSUSHITA ◽  
Kayoko YAMASHITA ◽  
Hiromi FURUICHI ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Calcium Binding ◽  
Binding Proteins ◽  
S100 Protein ◽  
Reversed Phase ◽  
Molecular Probes ◽  
Calcium Binding Proteins ◽  
Ige Mediated ◽  
Human And Mouse

To investigate the roles of calcium-binding proteins in degranulation, we used three anti-allergic drugs, amlexanox, cromolyn and tranilast, which inhibit IgE-mediated degranulation of mast cells, as molecular probes in affinity chromatography. All of these drugs, which have different structures but similar function, scarcely bound to calmodulin in bovine lung extract, but bound to the same kinds of calcium-binding proteins, such as the 10-kDa proteins isolated in this study, calcyphosine and annexins I–V. The 10-kDa proteins obtained on three drug-coupled resins and on phenyl-Sepharose were analysed by reversed-phase HPLC. It was found that two characteristic 10-kDa proteins, one polar and one less polar, were bound with all three drugs, although S100A2 (S100L), of the S100 family, was bound with phenyl-Sepharose. The cDNA and deduced amino acid sequence proved our major polar protein to be identical with the calcium-binding protein in bovine amniotic fluid (CAAF1, S100A12). The cDNA and deduced amino acid sequence of the less-polar protein shared 95% homology with human and mouse S100A13. In addition, it was demonstrated that the native S100A12 and recombinant S100A12 and S100A13 bind to immobilized amlexanox. On the basis of these findings, we speculate that the three anti-allergic drugs might inhibit degranulation by binding with S100A12 and S100A13.

Troponin C and calcium dependent regulator protein, two ancestral skeletal muscle calcium binding proteins

Biosystems ◽  
1980 ◽  
Vol 12 (3-4) ◽  
pp. 317-323 ◽  
Author(s):  
L.M.G. Heilmeyer ◽  
U. Jahnke ◽  
M.W. Kilimann ◽  
K.P. Kohse ◽  
J.E. Sperling ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Troponin C ◽  
Calcium Binding Proteins ◽  
Calcium Dependent ◽  
Regulator Protein ◽  
Muscle Calcium

Amino acid sequence of two sarcoplasmic calcium-binding proteins from the protochordate Amphioxus

Biochemistry ◽  
1986 ◽  
Vol 25 (12) ◽  
pp. 3585-3592 ◽  
Author(s):  
Takashi Takagi ◽  
Kazuhiko Konishi ◽  
Jos A. Cox
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins

The amino acid sequence of porcine intestinal calcium-binding protein

1979 ◽  
Vol 57 (6) ◽  
pp. 737-748 ◽  
Author(s):  
Theo Hofmann ◽  
Michiko Kawakami ◽  
Anthony J. W. Hitchman ◽  
Joan E. Harrison ◽  
Keith J. Dorrington
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intestinal Mucosa ◽  
Calcium Binding ◽  
Binding Protein ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

The complete amino acid sequence of the calcium-binding protein (CaBP) from pig intestinal mucosa has been determined: Ac-Ser-Ala-Gln-Lys-Ser-Pro-Ala-Glu-Leu-Lys-Ser-Ile-Phe-Glu-Lys-Tyr-Ala-Ala-Lys-Glu-Gly-Asp-Pro-Asn-Gln-Leu-Ser-Lys-Glu-Glu-Leu-Lys-Gln-Leu-Ile-Gln-Ala-Glu-Phe-Pro-Ser-Leu-Leu-Lys-Gly-Pro-Arg-Thr-Leu-Asp-Asp-Leu-Phe-Gln-Glu-Leu-Asp-Lys-Asn-Gly-Asn-Gly-Glu-Val-Ser-Phe-Glu-Glu-Phe-Gln-Val-Leu-Val-Lys-Lys-Ile-Ser-Gln-OH. The N-terminal octapeptide sequence was determined by mass spectrometry analysis by Morris and Dell. The first 45 residues of bovine CaBP differ only in six positions from the corresponding sequence of the porcine protein, except that the sequence starts in position two of the porcine sequence. The mammalian intestinal CaBP's belong to the troponin-C superfamily on the basis of an analysis by Barker and Dayhoff.

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