scholarly journals The purification and complete amino acid sequence of the 9000-Mr Ca2+-binding protein from rat placenta. Identity with the vitamin D-dependent intestinal Ca2+-binding protein

1986 ◽  
Vol 235 (2) ◽  
pp. 585-595 ◽  
Author(s):  
J P MacManus ◽  
D C Watson ◽  
M Yaguchi
Keyword(s):  
Vitamin D ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Protein ◽  
Protein A ◽  
Minor Component ◽  
Protein Residues ◽  
Complete Amino Acid Sequence ◽  
Placental Protein ◽  
A Minor

A 9000-Mr Ca2+-binding protein was isolated from rat placenta and purified to homogeneity by h.p.l.c. procedures. The complete amino acid sequence was established for the 78-residue placental protein. A sequence analysis of a minor component of the rat intestinal Ca2+-binding protein (residues 4-78) and a tryptic peptide (residues 55-74), both purified by h.p.l.c., showed both proteins to be identical. Thus this placental 9000-Mr Ca2+-binding protein is the same gene product as the intestinal Ca2+-binding protein whose synthesis is dependent on vitamin D.

scholarly journals Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of the human complement system

1985 ◽  
Vol 230 (1) ◽  
pp. 133-141 ◽  
Author(s):  
L P Chung ◽  
D R Bentley ◽  
K B Reid
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Protein A ◽  
Classical Pathway ◽  
Amino Acid Residues ◽  
Cloned Cdna

By using synthetic oligonucleotides as probes, plasmid clones containing portions of cDNA coding for human C4b-binding protein were isolated from a liver cDNA library. The entire amino acid sequence of the C4b-binding protein can be predicted from this study of the cloned cDNA when allied to a previous sequence study at the protein level [Chung, Gagnon & Reid (1985) Mol. Immunol. 22, 427-435], in which over 55% of the amino acid sequence, including the N-terminal 62 residues, was obtained. The plasmid clones isolated allowed the unambiguous determination of 1717 nucleotides of cDNA sequence between the codon for the 32nd amino acid in the sequence of C4b-binding protein and the 164th nucleotide in the 3′ non-translated region. The sequence studies show that the secreted form of C4b-binding protein, found in plasma, is composed of chains of apparent Mr 70 000 that contains 549 amino acid residues. Examination of the protein and cDNA sequence results show that there are at least two polymorphic sites in the molecule. One is at position 44, which can be glutamine or threonine, and the other is at position 309, which can be tyrosine or histidine. Northern-blot analysis indicated that the mRNA for C4b-binding protein is approx. 2.5 kilobases long. The N-terminal 491 amino acids of C4b-binding protein can be divided into eight internal homologous regions, each approx. 60 amino acids long, which can be aligned by the presence in each region of four half-cystine, one tryptophan and several other conserved residues. These regions in C4b-binding protein are homologous with the three internal-homology regions that have been reported to be present within the Ba region of the complement enzyme factor B and also to the internal-homology regions found in the non-complement beta 2-glycoprotein I.

scholarly journals Complete amino acid sequence of pyrazine-binding protein from cow nasal mucosa

1989 ◽  
Vol 185 (3) ◽  
pp. 569-572 ◽  
Author(s):  
Roberto TIRINDELLI ◽  
Jeffrey N. KEEN ◽  
Andrea CAVAGGIONI ◽  
Elias E. ELIOPOULOS ◽  
John B. C. FINDLAY
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Nasal Mucosa ◽  
Binding Protein ◽  
Complete Amino Acid Sequence

The DNA-binding protein II from Zymomonas mobilis. Complete amino acid sequence and interaction with DNA

Biochimie ◽  
1998 ◽  
Vol 80 (2) ◽  
pp. 109-116
Author(s):  
B. Laine ◽  
F. Chartier ◽  
F. Culard ◽  
D. Bélaïche ◽  
P. Sautière
Keyword(s):  
Amino Acid ◽  
Dna Binding ◽  
Amino Acid Sequence ◽  
Zymomonas Mobilis ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Complete Amino Acid Sequence

scholarly journals Studies on the high-sulphur proteins of reduced Merino wool. Amino acid sequence of protein SCMKB-IIIA3

1973 ◽  
Vol 133 (4) ◽  
pp. 641-654 ◽  
Author(s):  
Louis S. Swart ◽  
Thomas Haylett
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Minor Component ◽  
Amino Acid Sequences ◽  
Edman Degradation ◽  
Merino Wool ◽  
C Terminus ◽  
A Minor

The complete amino acid sequences of wool protein SCMKB-IIIA3 (131 residues) and a minor component SCMKB-IIIA3A (130 residues) have been determined. The proteins are mutually homologous and have free threonine as the N-terminal residue and carboxymethylcysteine as the C-terminus. The peptides used for the sequence work were obtained by trypsin, thermolysin, pepsin and chymotrypsin digestions and were fractionated by chromatography on DEAE-cellulose, gel filtration on Sephadex G-25 and G-50, paper chromatography and electrophoresis. The Edman degradation method (employing both the Beckman Sequencer and a non-automatic procedure) was used to obtain the sequences of the peptides.

Partial sequence of hemoglobin from cobra (Naja naja naja)

1987 ◽  
Vol 7 (10) ◽  
pp. 813-819 ◽  
Author(s):  
Sabira Naqvi ◽  
Iffat N. Nadvi ◽  
Zafar H. Zaidi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Minor Component ◽  
Partial Sequence ◽  
Terminal Amino Acid ◽  
Naja Naja ◽  
Terminal Amino ◽  
A Minor ◽  
Cellulose Column ◽  
Terminal Amino Acid Sequence

Hemoglobin from the cobra snake, Naja naja naja, was isolated and its chains separated on a CM-cellulose column. The separation profile revealed an α and two β chains having the molar proportions of [α]2,[β1]1,[β2]1. The N-terminal amino acid sequence of the intact chains and of the CNBr peptides were carried out. The β2 chain was found to be heterogeneous comprising a minor component amounting to 11%. This later showed changes at two positions 9 and 14 in the first 30 residues sequenced.

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