Amino acid sequence of crayfish (Astacus fluviatilis) carboxypeptidase B

Biochemistry ◽  
1984 ◽  
Vol 23 (6) ◽  
pp. 1245-1250 ◽  
Author(s):  
Koiti Titani ◽  
Lowell H. Ericsson ◽  
Santosh Kumar ◽  
Frank Jakob ◽  
Hans Neurath ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Carboxypeptidase B ◽  
Astacus Fluviatilis

Amino acid sequence of crayfish (Astacus fluviatilis) trypsin If

Biochemistry ◽  
1983 ◽  
Vol 22 (6) ◽  
pp. 1459-1465 ◽  
Author(s):  
Koiti Titani ◽  
Tatsuru Sasagawa ◽  
Richard G. Woodbury ◽  
Lowell H. Ericsson ◽  
Herbert Dorsam ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Astacus Fluviatilis

scholarly journals Purification of carboxypeptidase B from human pancreas

1977 ◽  
Vol 163 (2) ◽  
pp. 253-260 ◽  
Author(s):  
D V Marinkovic ◽  
J N Marinkovic ◽  
E G Erdös ◽  
C J G Robinson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sodium Dodecyl ◽  
Deae Cellulose ◽  
Amino Acid Content ◽  
Disc Electrophoresis ◽  
Human Pancreas ◽  
Peptidase Activity ◽  
Ph Optimum ◽  
Carboxypeptidase B

Carboxypeptidase B of the human pancreas was purified by chromatography on DEAE-cellulose and CM-cellulose columns. Two forms of the enzyme, named carboxypeptidase B1 and B2, were separated. They have similar mol.wts. (34250 +/- 590) as established by polyacrylamide-gel disc electrophoresis and by gel filtration. Carboxypeptidase B2 migrates further towards the anode in disc electrophoresis. When the amino acid content of the enzymes was analysed, carboxypeptidase B2 had four more glycine and three more aspartic acid residues than had form B1. The amino acid sequence of the human carboxypeptidase B1 differs from that of the bovine enzyme only in two places in the N-terminal 20-amino-acid sequence. The N-terminal amino acid in carboxypeptidase B1 and B2 is alanine. The peptide ‘map’ of the tryptic digest of carboxypeptidase B1 contained more peptides than did that of form B2. The Km, the Vmax. and the pH optimum of the cleavage of the peptide substrate hippurylarginine and the ester substrate hippurylargininic acid were similar for both enzymes. CoCl2 accelerated the peptidase activity, and cadmium acetate enhanced the esterase activity, of human carboxypeptidases B1 and B2. Urea and sodium dodecyl sulphate inhibited the enzymes.

Amino acid sequence of a unique protease from the crayfish Astacus fluviatilis

Biochemistry ◽  
1987 ◽  
Vol 26 (1) ◽  
pp. 222-226 ◽  
Author(s):  
Koiti Titani ◽  
Hans Joachim Torff ◽  
Scott Hormel ◽  
Santosh Kumar ◽  
Kenneth A. Walsh ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Astacus Fluviatilis

scholarly journals Amino-acid sequence of bovine carboxypeptidase B.

1975 ◽  
Vol 72 (5) ◽  
pp. 1666-1670 ◽  
Author(s):  
K. Titani ◽  
L. H. Ericsson ◽  
K. A. Walsh ◽  
H. Neurath
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Carboxypeptidase B

scholarly journals Confirmation of the 1–20 amino acid sequence of human adrenocorticotrophin

1973 ◽  
Vol 133 (1) ◽  
pp. 11-13 ◽  
Author(s):  
H. P. J. Bennett ◽  
P. J. Lowry ◽  
C. McMartin
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Countercurrent Distribution ◽  
Edman Degradation ◽  
Sequence Determination ◽  
Carboxypeptidase B ◽  
Aminopeptidase M

The tryptic fragments of natural human adrenocorticotrophin, were separated by countercurrent distribution and a correction in positions 25, 26, 27 and 30 was made by Riniker et al. (1972) in a study of the fragment containing residues 22–39. We have purified the remaining tryptic fragments, namely residues 1–8, 9–15, 16–21 and 17–21, by using ion-exchange chromatography on CM-cellulose and have carried out sequence determination by using the subtractive Edman degradation procedure and digestion with aminopeptidase M and carboxypeptidase B. These results have confirmed the proposed sequence for human adrenocorticotrophin in regions 6–7, 10–14 and 17–20, which had previously been arrived at only by analogy with the invariant sequence found in the three other mammalian adrenocorticotrophin species that had been investigated.

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

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.

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.

Paris I Dysfibrinogenemia: A Point Mutation in Intron 8 Results in Insertion of a 15 Amino Acid Sequence in the Fibrinogen γ-Chain

1993 ◽  
Vol 69 (03) ◽  
pp. 217-220 ◽  
Author(s):  
Jonathan B Rosenberg ◽  
Peter J Newman ◽  
Michael W Mosesson ◽  
Marie-Claude Guillin ◽  
David L Amrani
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Point Mutation ◽  
Genomic Dna ◽  
Comparative Sequence Analysis ◽  
Chain Gene ◽  
Molecular Defect ◽  
Nucleotide Position ◽  
Normal Individuals ◽  
Polymerase Chain

SummaryParis I dysfibrinogenemia results in the production of a fibrinogen molecule containing a functionally abnormal γ-chain. We determined the basis of the molecular defect using polymerase chain reaction (PCR) to amplify the γ-chain region of the Paris I subject’s genomic DNA. Comparative sequence analysis of cloned PCR segments of normal and Paris I genomic DNA revealed only an A→G point mutation occurring at nucleotide position 6588 within intron 8 of the Paris I γ-chain gene. We examined six normal individuals and found only normal sequence in this region, indicating that this change is not likely to represent a normal polymorphism. This nucleotide change leads to a 45 bp fragment being inserted between exons 8 and 9 in the mature γparis I chain mRNA, and encodes a 15 amino acid insert after γ350 [M-C-G-E-A-L-P-M-L-K-D-P-C-Y]. Alternative splicing of this region from intron 8 into the mature Paris I γ-chain mRNA also results after translation into a substitution of S for G at position γ351. Biochemical studies of 14C-iodoacetamide incorporation into disulfide-reduced Paris I and normal fibrinogen corroborated the molecular biologic predictions that two additional cysteine residues exist within the γpariS I chain. We conclude that the insertion of this amino acid sequence leads to a conformationallyaltered, and dysfunctional γ-chain in Paris I fibrinogen.

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.

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