The Amino Acid Sequence of Porcine Thyrotropin with Reference to the Molecular Evolution of Glycoprotein Hormones

1974 ◽  
Vol 2 (5) ◽  
pp. 912-913 ◽  
Author(s):  
JEAN CLOSSET ◽  
G. MAGHUIN-ROGISTER ◽  
GEORGES HENNEN
Keyword(s):  
Amino Acid ◽  
Molecular Evolution ◽  
Amino Acid Sequence ◽  
Glycoprotein Hormones

Rates of Albumin Evolution in Parrots (Aves, Psittaciformes)

1992 ◽  
Vol 40 (3) ◽  
pp. 313 ◽  
Author(s):  
PR Baverstock ◽  
L Christidis ◽  
M Krieg ◽  
J Birrell
Keyword(s):  
Amino Acid ◽  
Molecular Evolution ◽  
Amino Acid Sequence ◽  
Sequence Divergence ◽  
Modern Distribution ◽  
Rate Of Molecular Evolution ◽  
Microcomplement Fixation ◽  
Amino Acid Sequence Divergence ◽  
Lines Of Evidence

A number of lines of evidence suggest that the rate of molecular evolution in birds is slower than in other vertebrates. This hypothesis was tested by measuring the extent of amino-acid sequence divergence in albumin among species of parrots by means of microcomplement fixation. This group was chosen because its modern distribution is strongly suggestive of a Gondwanan origin. The results show that the intercontinental albumin distances are well below those expected for a Gondwanan group. These data are in accord with the hypothesis that birds have a slower rate of molecular evolution, although other explanations are possible.

scholarly journals Molecular Evolution of the H-NS Protein: Interaction with Hha-Like Proteins Is Restricted to Enterobacteriaceae

2006 ◽  
Vol 189 (1) ◽  
pp. 265-268 ◽  
Author(s):  
Cristina Madrid ◽  
Jesús García ◽  
Miquel Pons ◽  
Antonio Juárez
Keyword(s):  
Amino Acid ◽  
Molecular Evolution ◽  
Amino Acid Sequence ◽  
Protein Interaction ◽  
Terminal Domain ◽  
Key Residues

ABSTRACT We show here that chromosomal hha-like genes are restricted to the Enterobacteriaceae. The H-NS N-terminal domain of members of this family includes an unaltered seven-amino-acid sequence located between helixes 1 and 2, termed the Hha signature, that contains key residues for H-NS-Hha interaction.

The primary structure of carp myoglobin in the context of molecular evolution

1982 ◽  
Vol 297 (1084) ◽  
pp. 1-25 ◽  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Molecular Evolution ◽  
Amino Acid Sequence ◽  
Neutral Theory ◽  
Amino Acid Substitutions ◽  
Biochemical Evolution ◽  
Constant Rate ◽  
Rate Of Molecular Evolution ◽  
Living Species

The amino acid sequence of skeletal muscle myoglobin from carp ( Cyprinus carpio ) is presented. Comparisons are made with previously reported myoglobin sequences for several other fish and birds, and many mammals. The functional significance of the amino acid substitutions and ‘deletions’ in the carp sequence is considered. The new sequence is used in a re-examination of the evidence for an approximately constant rate of molecular evolution. By using estimates of the dates of divergence of lineages leading to living species and equations put forward by proponents of the ‘neutral theory’ of biochemical evolution it is demonstrated that similar amounts of change appear to have occurred over periods of time that differ by more than a factor of two.

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.

Sign in / Sign up

Export Citation Format

Share Document