Amino acid sequence of a vitamin K-dependent Ca2+-binding peptide from bovine prothrombin.

Abstract The 32 kDa herbicide and QB binding peptide (D-1 protein) and its homologous 34 kDa peptide (D-2 protein) are integral membrane subunits of photosystem II. A model for their folding through the thylakoid membrane in five transmembrane a-helices is proposed from the comparison of amino acid sequence and hydropathy index plot homologies with subunits of the bacterial system. Following recent data on the X-ray structure of a bacterial photosystem the binding niche for QB is interpreted on the basis of the amino acid changes found in the 32 kDa peptide in herbicide tolerant higher plants and algae.

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Comparison of amino acid sequence of bovine coagulation Factor IX (Christmas Factor) with that of other vitamin K-dependent plasma proteins.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.76.10.4990 ◽

1979 ◽

Vol 76 (10) ◽

pp. 4990-4994 ◽

Cited By ~ 89

Author(s):

K. Katayama ◽

L. H. Ericsson ◽

D. L. Enfield ◽

K. A. Walsh ◽

H. Neurath ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Vitamin K ◽

Plasma Proteins ◽

Coagulation Factor ◽

Factor Ix ◽

Coagulation Factor Ix

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The Amino-Acid Sequence of the Vitamin-K-Dependent Part of Protein Z

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1982.tb06785.x ◽

2005 ◽

Vol 126 (2) ◽

pp. 346-348

Author(s):

Peter Højrup ◽

Peter Roepstorff ◽

Torben E. Petersen

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Vitamin K ◽

Protein Z ◽

Dependent Part

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Amino acid sequence of cadmium-binding peptide induced in a marine diatom,Phaeodactylum tricornutum

Bulletin of Environmental Contamination and Toxicology ◽

10.1007/bf01701090 ◽

1990 ◽

Vol 45 (6) ◽

pp. 893-899 ◽

Cited By ~ 8

Author(s):

S. Kawaguchi ◽

Y. Maita

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Phaeodactylum Tricornutum ◽

Marine Diatom ◽

Binding Peptide

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The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142372 ◽

1986 ◽

Vol 44 ◽

pp. 150-151

Author(s):

M.K. Lamvik ◽

L.L. Klatt

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Staining Pattern ◽

Banding Patterns ◽

Mass Thickness ◽

New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

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Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

Thrombosis and Haemostasis ◽

10.1055/s-0038-1646610 ◽

1989 ◽

Vol 61 (03) ◽

pp. 437-441 ◽

Cited By ~ 28

Author(s):

Cindra Condra ◽

Elka Nutt ◽

Christopher J Petroski ◽

Ellen Simpson ◽

P A Friedman ◽

...

Keyword(s):

Molecular Weight ◽

Salivary Gland ◽

Amino Acid ◽

Amino Acid Sequence ◽

Western Blot ◽

Potent Inhibitor ◽

Factor Xa ◽

Coagulation Factor ◽

Sds Page ◽

Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

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