Disulfide bonds of basic acrosin inhibitor (BUSI II) from bull seminal plasma

1984 ◽  
Vol 49 (5) ◽  
pp. 1204-1210 ◽  
Author(s):  
Alena Rzavská ◽  
Bedřich Meloun ◽  
Dana Čechová
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Disulfide Bonds ◽  
Cysteine Residues ◽  
Chromatographic Techniques

The thermolysin digest of the basic acrosin inhibitor (molecular weight 6 200) was resolved on a column of Sephadex G-15 and subsequently by electrophoretic and chromatographic techniques. Cysteine peptides, which link together half-cysteine residues 7 and 39, 17 and 36, and 25 and 57 by disulfide bonds, were isolated. The structure of the molecule of the basic acrosin inhibitor corresponds to structures of inhibitors of the Kazal type. The amino acid sequence of a few residues in the basic acrosin inhibitor has been revised.

Amino acid sequence of the acidic acrosin inhibitor (BUSI I B2) from bull seminal plasma

1983 ◽  
Vol 48 (9) ◽  
pp. 2558-2568 ◽  
Author(s):  
Bedřich Meloun ◽  
Věra Jonáková ◽  
Dana Čechová
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Sequential Data ◽  
Amino Acid Residues

The molecule of the inhibitor consists of 63 amino acid residues whose sequence is the following: Glu-Ile-Tyr-Phe-Glu-Pro-Asp-Phe-Gly-Phe-Pro-Pro-Asp-Cys-Lys-Val-Tyr-Thr-Glu-Ala-Cys-Thr-Arg-Glu-Tyr-Asn-Pro-Ile-Cys-Asp-Ser-Ala-Ala-Lys-Thr-Tyr-Ser-Asn-Glu-Cys-Thr-Phe-Cys-Asn-Glu-Lys-Met-Asn-Asn-Asp-Ala-Asp-Ile-His-Phe-Gln-His-Phe-Gly-Glu-Cys-Glu-Tyr. The sequential data were obtained by the analysis of peptides isolated from the tryptic and chymotryptic digest of the carboxymethylated inhibitor. The molecular weight of the inhibitor calculated from its amino acid sequence is 7377.

scholarly journals Immunoglobulin λ-chains. The complete amino acid sequence of a Bence-Jones protein

1968 ◽  
Vol 110 (4) ◽  
pp. 631-652 ◽  
Author(s):  
C. Milstein ◽  
J. B. Clegg ◽  
J. M. Jarvis
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Total Amino Acid ◽  
Cysteine Residues ◽  
Bence Jones Protein ◽  
Chromatographic Techniques ◽  
Peptic Digestion ◽  
Similarities And Differences ◽  
Methionine Residues ◽  
Bence Jones Proteins

The total amino acid sequence of a λ Bence-Jones protein has been established. The protein contains 211 residues, which include two methionine residues. Splitting with cyanogen bromide gave three fragments, the largest of which included the C-terminal half, which is common to other Bence-Jones proteins of the same type. The peptides obtained by tryptic, chymotryptic and peptic digestion were isolated and purified by paper-electrophoretic and chromatographic techniques. Reduction followed by carboxymethylation of the cysteine residues with radioactive iodoacetate was found to be a powerful tool in the isolation of some insoluble peptides. Unusual features of the molecule are the fact that it contains six cysteine residues and not five as observed in both κ and λ Bence-Jones proteins studied previously, and its size, which seems two residues smaller than the smallest Bence-Jones protein studied hitherto. The similarities and differences between this and other Bence-Jones proteins are discussed.

Amino acid sequence of basic acrosin inhibitor from bull seminal plasma

1979 ◽  
Vol 44 (9) ◽  
pp. 2710-2721 ◽  
Author(s):  
Bedřich Meloun ◽  
Dana Čechová
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Carboxylic Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Terminal Group ◽  
Sequential Data ◽  
Amino Acid Residues ◽  
Pyrrolidone Carboxylic Acid

The molecule of the inhibitor contains 57 amino acid residues whose sequence is the following: Pyr-Gly-Ala-Gln-Val-Asp-Cys-Ala-Glu-Phe-Lys-Asp-Pro-Lys-Val-Tyr-Cys-Thr-Arg-His-Ser-Asp-Pro-Gln-Cys-Gly-Ser-Asn-Gly-Glu-Thr-Tyr-Gly-Asn-Lys-Cys-Ala-Phe-Cys-Lys-Ala-Val-Met-Lys-Ser-Gly-Gly-Lys-Ile-Asn-Leu-Lys-His-Arg-Gly-Cys-Lys. The N-terminal group of the inhibitor is pyrrolidone carboxylic acid. The sequential data were obtained by analyses of peptides isolated from tryptic and chymotryptic digests of the oxidized or carboxymethylated inhibitor. The molecular weight of the inhibitor is 6 200.

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.

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

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.

Molecular analysis of nuc-1+, a gene controlling phosphorus acquisition in Neurospora crassa

1990 ◽  
Vol 10 (11) ◽  
pp. 5839-5848
Author(s):  
S Kang ◽  
R L Metzenberg
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Phosphorus Acquisition ◽  
Regulatory Factor ◽  
Physical Interactions ◽  
Negative Regulatory Factor ◽  
High Phosphate

In response to phosphorus starvation, Neurospora crassa makes several enzymes that are undetectable or barely detectable in phosphate-sufficient cultures. The nuc-1+ gene, whose product regulates the synthesis of these enzymes, was cloned and sequenced. The nuc-1+ gene encodes a protein of 824 amino acids with a predicted molecular weight of 87,429. The amino acid sequence shows homology with two yeast proteins whose functions are analogous to that of the NUC-1 protein. Two nuc-1+ transcripts of 3.2 and 3.0 kilobases were detected; they were present in similar amounts during growth at low or high phosphate concentrations. The nuc-2+ gene encodes a product normally required for NUC-1 function, and yet a nuc-2 mutation can be complemented by overexpression of the nuc-1+ gene. This implies physical interactions between NUC-1 protein and the negative regulatory factor(s) PREG and/or PGOV. Analysis of nuc-2 and nuc-1; nuc-2 strains transformed by the nuc-1+ gene suggests that phosphate directly affects the level or activity of the negative regulatory factor(s) controlling phosphorus acquisition.

scholarly journals Molecular analysis of nuc-1+, a gene controlling phosphorus acquisition in Neurospora crassa.

1990 ◽  
Vol 10 (11) ◽  
pp. 5839-5848 ◽  
Author(s):  
S Kang ◽  
R L Metzenberg
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Phosphorus Acquisition ◽  
Regulatory Factor ◽  
Physical Interactions ◽  
Negative Regulatory Factor ◽  
High Phosphate

In response to phosphorus starvation, Neurospora crassa makes several enzymes that are undetectable or barely detectable in phosphate-sufficient cultures. The nuc-1+ gene, whose product regulates the synthesis of these enzymes, was cloned and sequenced. The nuc-1+ gene encodes a protein of 824 amino acids with a predicted molecular weight of 87,429. The amino acid sequence shows homology with two yeast proteins whose functions are analogous to that of the NUC-1 protein. Two nuc-1+ transcripts of 3.2 and 3.0 kilobases were detected; they were present in similar amounts during growth at low or high phosphate concentrations. The nuc-2+ gene encodes a product normally required for NUC-1 function, and yet a nuc-2 mutation can be complemented by overexpression of the nuc-1+ gene. This implies physical interactions between NUC-1 protein and the negative regulatory factor(s) PREG and/or PGOV. Analysis of nuc-2 and nuc-1; nuc-2 strains transformed by the nuc-1+ gene suggests that phosphate directly affects the level or activity of the negative regulatory factor(s) controlling phosphorus acquisition.

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