Amino acid sequence of the light chain of bovine factor X1 (Stuart factor)

Enfield, David L.; Ericsson, Lowell H.; Fujikawa, Kazuo; Walsh, Kenneth A.; Neurath, Hans; Titani, Koiti

doi:10.1021/bi00545a009

Cited by 62 publications

(30 citation statements)

References 60 publications

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“…The protein was then treated with 4-vinylpyridine under reducing conditions to alkylate the cysteine residues, as described by Enfield et al (1980), TCA-precipitated, acetone-washed, and resuspended in 200 ~1 of 70% formic acid. CNBr {1 rag) was added, and the mixture incubated for 36 hr at room temperature in the dark under nitrogen.…”

Section: Ap-2 Purification and Peptide Sequencingmentioning

confidence: 99%

Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements.

Williams

Admon

Lüscher³

et al. 1988

Genes & Development

568

357

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Section: Ap-2 Purification and Peptide Sequencingmentioning

confidence: 99%

Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements.

Williams

Admon

Lüscher³

et al. 1988

Genes & Development

568

357

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“…The reaction was stopped by dilution with water (1: 10) and the sample was freeze-dried. Cleavage at the Asn-Gly bond by hydroxylamine was carried out as described in [14], except that the protein was dissolved in 1% SDS instead of in guanidinium-HCl and a pH of 10 was used.…”

Section: Chemical Cleavagesmentioning

confidence: 99%

The ADP/ATP carrier from yeast (AAC‐2) is uniquely suited for the assignment of the binding center by photoaffinity labeling

1989

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The ADP/ATP carrier from yeast was photoaffinity-labeled in mitochondria with 2-azido-[a-32P]ATP in a binding-centerspecific, i.e. carboxyatractylate-sensitive, manner. After isolation, fragmentation possibilities unique for the yeast AAC-2 could be exploited to assign the insertion to a narrow range of the sequence. The CNBr fragment 115-2.lO contained all the incorporated label which corresponds to the second domain within the triple-domain primary structure of the AAC. With hydroxylamine cleavage directed to the Asn 171-Gly 172 site, all the label was found in the C-terminal 16 kDa fragment. Thus the 2-azido-ATP incorporation is clearly delimited to the 172-210 segment. 8-Azido-[a-3ZP]ATP could be site-specifically incorporated only in isolated AAC since it has a much lower affinity for AAC than 2-azido-ATP. The label was also exclusively found in the 172-210 region. With both forms no incorporation into the C-terminal region was found, as claimed for bovine AAC. The labeled segment contains Lys 179 and 182 which are homologous to bovine Lys 162 and 165 and which have been proposed to be in the translocation path.

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“…Factor X has been purified to homogeneity from both bovine (3) and human plasma (4) and consists of a light chain and a heavy chain linked by a disulfide bond. The complete amino acid sequences of the light and heavy chains of bovine factor X have been reported (5,6), as well as the complete amino acid sequence of the light chain of human factor X (7). The light chain of human factor X contains 11 residues of y-carboxyglutamic acid, which function in the binding of calcium ions (8), and a single residue of,8-hydroxyaspartic acid (7,9), the function of which is unclear.…”

mentioning

confidence: 99%

Characterization of an almost full-length cDNA coding for human blood coagulation factor X.

Fung¹,

Hay²,

MacGillivray³

1985

Proc. Natl. Acad. Sci. U.S.A.

121

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A human liver cDNA library was screened by colony hybridization with a bovine factor X cDNA probe. Three of the positive plasmids contained overlapping DNA that coded for most of human factor X mRNA. DNA sequence analysis of these three clones allowed the prediction of the complete amino acid sequence of plasma factor X. From these studies, we predict that human factor X is synthesized as a single poly, peptide chain precursor in which the light and heavy chains of plasma factor X are linked by the tripeptide Arg-Lys-Arg. The cDNA sequence also predicts that human factor X is synthesized as a preproprotein having an amino-terminal leader peptide of at least 28 amino acid residues. A comparison of the amino acid sequences of human and bovine factor X shows high sequence identity around the calcium-binding regions and catalytic regions but low sequence identity around the nonfunctional regions.

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Amino acid sequence of the light chain of bovine factor X1 (Stuart factor)

Cited by 62 publications

References 60 publications

Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements.

Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements.

The ADP/ATP carrier from yeast (AAC‐2) is uniquely suited for the assignment of the binding center by photoaffinity labeling

Characterization of an almost full-length cDNA coding for human blood coagulation factor X.

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