scholarly journals Isolation of a new member of the S100 protein family: amino acid sequence, tissue, and subcellular distribution.

1989 ◽  
Vol 108 (2) ◽  
pp. 569-578 ◽  
Author(s):  
J R Glenney ◽  
M S Kindy ◽  
L Zokas
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Cell Line ◽  
Light Chain ◽  
Subcellular Distribution ◽  
S100 Protein ◽  
Protein Family ◽  
Striking Similarity ◽  
Bovine Kidney

A low molecular mass protein which we term S100L was isolated from bovine lung. S100L possesses many of the properties of brain S100 such as self association, Ca++-binding (2 sites per subunit) with moderate affinity, and exposure of a hydrophobic site upon Ca++-saturation. Antibodies to brain S100 proteins, however, do not cross react with S100L. Tryptic peptides derived from S100L were sequenced revealing similarity to other members of the S100 family. Oligonucleotide probes based on these sequences were used to screen a cDNA library derived from a bovine kidney cell line (MDBK). A 562-nucleotide cDNA was sequenced and found to contain the complete coding region of S100L. The predicted amino acid sequence displays striking similarity, yet is clearly distinct from other members of the S100 protein family. Polyclonal and monoclonal antibodies were raised against S100L and used to determine the tissue and subcellular distribution of this molecule. The S100L protein is expressed at high levels in bovine kidney and lung tissue, low levels in brain and intestine, with intermediate levels in muscle. The MDBK cell line was found to contain both S100L and the calpactin light chain, another member of this protein family. S100L was not found associated with a higher molecular mass subunit in MDBK cells while the calpactin light chain was tightly bound to the calpactin heavy chain. Double label immunofluorescence microscopy confirmed the observation that the calpactin light chain and S100L have a different distribution in these cells.

Amino Acid Sequence of the Light Chain of Human Low Molecular Mass Kininogen

1986 ◽  
pp. 91-95
Author(s):  
Friedrich Lottspeich ◽  
Josef Kellermann ◽  
Agnes Henschen ◽  
Günther Rauth ◽  
Werner Müller-Esterl
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Light Chain

scholarly journals The amino acid sequence of the light chain of human high-molecular-mass kiniogen

1985 ◽  
Vol 152 (2) ◽  
pp. 307-314 ◽  
Author(s):  
Friedrich LOTTSPEICH ◽  
Josef KELLERMANN ◽  
Agnes HENSCHEN ◽  
Berthold FOERTSCH ◽  
Werner MuLLER-ESTERL
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Light Chain ◽  
High Molecular Mass

Amino Acid Sequence of the Light Chain of Human High Molecular Mass Kininogen

1986 ◽  
pp. 85-89 ◽  
Author(s):  
Josef Kellermann ◽  
Friedrich Lottspeich ◽  
Agnes Henschen ◽  
Werner Müller-Esterl
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Light Chain ◽  
High Molecular Mass

scholarly journals Human low-molecular-mass kininogen. Amino-acid sequence of the light chain; homology with other protein sequences

1984 ◽  
Vol 142 (2) ◽  
pp. 227-232 ◽  
Author(s):  
Friedrich LOTTSPEICH ◽  
Josef KELLERMANN ◽  
Agnes HENSCHEN ◽  
Gunther RAUTH ◽  
Werner MULLER-ESTERL
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Light Chain ◽  
Protein Sequences

Identification of the gene encoding 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase in Burkholderia sp. HME13

2020 ◽  
Vol 85 (3) ◽  
pp. 626-629
Author(s):  
Hisashi Muramatsu ◽  
Hiroki Maguchi ◽  
Taisuke Harada ◽  
Takehiro Kashiwagi ◽  
Chul-Sa Kim ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Propionic Acid ◽  
Unknown Function ◽  
Protein Family ◽  
Amino Acid Sequence Analysis ◽  
Gene Encoding

ABSTRACT Here, we report the identification of the gene encoding a novel enzyme, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, in Burkholderia sp. HME13. The enzyme converts 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid and H2O to 3-(2,5-dioxoimidazolidin-4-yl) propionic acid and H2S. Amino acid sequence analysis of the enzyme indicates that it belongs to the DUF917 protein family, which consists of proteins of unknown function.

scholarly journals Amino acid sequence of the light chain of bovine protein C.

1982 ◽  
Vol 257 (20) ◽  
pp. 12170-12179 ◽  
Author(s):  
P Fernlund ◽  
J Stenflo
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Protein C

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.

scholarly journals The amino acid sequence of a lamba light chain presenting abnormal physicochemical and antigenic features

1985 ◽  
Vol 150 (2) ◽  
pp. 349-357 ◽  
Author(s):  
Edith MIHAESCO ◽  
Jean-Pierre ROY ◽  
Nicole CONGY ◽  
Liliane PERAN-RIVAT ◽  
Constantin MIHAESCO
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain

Physicochemical properties of a novel α-L-arabinofuranosidase fromRhizomucor pusillusHHT-1

2001 ◽  
Vol 47 (8) ◽  
pp. 767-772 ◽  
Author(s):  
A KM Shofiqur Rahman ◽  
Shinya Kawamura ◽  
Masahiro Hatsu ◽  
M M Hoq ◽  
Kazuhiro Takamizawa
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Gel Filtration ◽  
Hydrolytic Activity ◽  
Exchange Chromatography ◽  
Ph Optimum ◽  
Rhizomucor Pusillus ◽  
Terminal Amino ◽  
Metal Cofactors

The zygomycete fungus Rhizomucor pusillus HHT-1, cultured on L(+)arabinose as a sole carbon source, produced extracellular α-L-arabinofuranosidase. The enzyme was purified by (NH4)2SO4fractionation, gel filtration, and ion exchange chromatography. The molecular mass of this monomeric enzyme was 88 kDa. The native enzyme had a pI of 4.2 and displayed a pH optimum and stability of 4.0 and 7.0–10.0, respectively. The temperature optimum was 65°C, and it was stable up to 70°C. The Kmand Vmaxfor p-nitrophenyl α-L-arabinofuranoside were 0.59 mM and 387 µmol·min–1·mg–1protein, respectively. Activity was not stimulated by metal cofactors. The N-terminal amino acid sequence did not show any similarity to other arabinofuranosidases. Higher hydrolytic activity was recorded with p-nitrophenyl α-L-arabinofuranoside, arabinotriose, and sugar beet arabinan; lower hydrolytic activity was recorded with oat–spelt xylan and arabinogalactan, indicating specificity for the low molecular mass L(+)-arabinose containing oligosaccharides with furanoside configuration.Key words: α-L-arabinofuranosidase, enzyme purification, amino acid sequence, Rhizomucor pusillus.

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