scholarly journals Amino acid sequence of the carboxy-terminal part of an acidic type I cytokeratin of molecular weight 51 000 from Xenopus laevis epidermis as predicted from the cDNA sequence.

1984 ◽  
Vol 3 (6) ◽  
pp. 1301-1306 ◽  
Author(s):  
W. Hoffmann ◽  
J.K. Franz
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Xenopus Laevis ◽  
Cdna Sequence ◽  
Type I ◽  
Terminal Part ◽  
Carboxy Terminal ◽  
Acidic Type

scholarly journals Amino acid sequence microheterogeneities of a type I cytokeratin of M r 51 000 from Xenopus laevis epidermis

FEBS Letters ◽  
1988 ◽  
Vol 237 (1-2) ◽  
pp. 178-182 ◽  
Author(s):  
Werner Hoffmann ◽  
Sylvia Sterrer ◽  
Andreas Königstorfer
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Xenopus Laevis ◽  
Type I

scholarly journals A Xenopus laevis creatine kinase isozyme (CK-III/III) expressed preferentially in larval striated muscle: cDNA sequence, developmental expression and subcellular immunolocalization

1991 ◽  
Vol 58 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Jacques Robert ◽  
Benjamin Barandun ◽  
Hans Rudolf Kobel
Keyword(s):  
Creatine Kinase ◽  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Xenopus Laevis ◽  
Tissue Distribution ◽  
Cdna Sequence ◽  
Striated Muscle ◽  
Developmental Expression ◽  
Myoblast Differentiation

SummaryA cDNA containing the nearly complete coding sequence of CK-III subunit of X. laevis was isolated, sequenced and further identified by comparing the tissue distribution of CK-III/III isozyme with that of its messenger. Comparison of CK-III deduced amino acid sequence with other CK sequences published reveals its close homology to M-CK subunits. Results using both cDNA probes and monoclonal antibodies specific for CK-III subunits indicate that the appearance and the accumulation of CK-III occur in parallel with myoblast differentiation. Moreover, subcellular immuno-histolocalization shows that CK-III/III isozyme is especially concentrated on larval myofibres at the level of A-bands.

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

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
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.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

scholarly journals The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Molecular Weight ◽  
Complete Amino Acid Sequence

cDNA Sequence and Deduced Amino Acid Sequence of a Fungal Stress Protein Induced inRhizopus nigricansby Steroids

1998 ◽  
Vol 250 (3) ◽  
pp. 664-667 ◽  
Author(s):  
Bronislava Črešnar ◽  
Andreja Plaper ◽  
Katja Breskvar ◽  
Tamara Hudnik-Plevnik
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Sequence ◽  
Stress Protein

scholarly journals Crotalase, a Fibrinogen-Clotting Snake Venom Enzyme: Primary Structure and Evidence for a Fibrinogen Recognition Exosite Different from Thrombin

1999 ◽  
Vol 81 (01) ◽  
pp. 81-86 ◽  
Author(s):  
Agnes Henschen-Edman ◽  
Ida Theodor ◽  
Brian Edwards ◽  
Hubert Pirkle
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Spatial Modeling ◽  
Glycosylation Site ◽  
Amino Sugars ◽  
Edman Degradation ◽  
Heparin Binding ◽  
Heparin Binding Site ◽  
Total Molecular Weight

SummaryCrotalase, a fibrinogen-clotting enzyme isolated from the venom of Crotalus adamanteus, and its overlapping fragments were subjected to Edman degradation. The resulting amino acid sequence, VIGGDEC NINEHRFLVALYDYWSQLFLCGGTLINNEWVLTAAHCDRTHI LIYVGVHDRSVQFDKEQRRFPKEKYFFDCSNNFTKWDKDIM LIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRAMGWGQTTSPQET LPDVPHCANINLLDYEVCRTAHPQFRLPATSRTLCAGVLEG GIDTCNRDSGGPLICNGQFQGIVFWGPDPCAQPDKPGLYTK VFDHLDWIQSIIAGEKTVNCP, is characteristic of a serine protein-ase. Comparison with thrombin, the physiological fibrinogen-clotting enzyme, showed that thrombin’s fibrinogen-recognition exosite (FRE) is poorly represented in crotalase. Hirudin, a FRE-dependent inhibitor, had no effect on crotalase. Spatial modeling of crotalase yielded a possible alternative fibrinogen-recognition site comprised of Arg 60F, Lys 85, Lys 87, and Arg 107 (underlined in the sequence above). Crotalase also lacks thrombin’s YPPW loop, as well as its functionally important ETW 146-148, and its heparin-binding site. The enzyme contains a single asparagine-linked glycosylation site, NFT, bearing neutral and amino sugars that account for 8.3% of the enzyme’s total molecular weight of 29,027. The calculated absorbance of crotalase at 280 nm, 1%, cm-1is 15.2.

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