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

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.

Download Full-text

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

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)33696-2 ◽

1982 ◽

Vol 257 (20) ◽

pp. 12170-12179 ◽

Cited By ~ 20

Author(s):

P Fernlund ◽

J Stenflo

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Light Chain ◽

Protein C

Download Full-text

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

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1985.tb09027.x ◽

1985 ◽

Vol 150 (2) ◽

pp. 349-357 ◽

Cited By ~ 4

Author(s):

Edith MIHAESCO ◽

Jean-Pierre ROY ◽

Nicole CONGY ◽

Liliane PERAN-RIVAT ◽

Constantin MIHAESCO

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Light Chain

Download Full-text

Partial amino-acid sequence of the precursor of an immunoglobulin light chain containing NH2-terminal pyroglutamic acid.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.73.8.2604 ◽

1976 ◽

Vol 73 (8) ◽

pp. 2604-2608 ◽

Cited By ~ 22

Author(s):

Y. Burstein ◽

F. Kantour ◽

I. Schechter

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Light Chain ◽

Pyroglutamic Acid ◽

Immunoglobulin Light Chain ◽

Partial Amino Acid Sequence

Download Full-text

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

Canadian Journal of Microbiology ◽

10.1139/w01-064 ◽

2001 ◽

Vol 47 (8) ◽

pp. 767-772 ◽

Cited By ~ 2

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 7.010.0, 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·min1·mg1protein, 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 oatspelt 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.

Download Full-text