Amino-Acid Sequence Around the Reactive Thiol Groups of Adenosine Triphosphate–creatine Phosphotransferase

Nature ◽  
1964 ◽  
Vol 203 (4942) ◽  
pp. 267-269 ◽  
Author(s):  
A. R. THOMSON ◽  
J. W. EVELEIGH ◽  
B. J. MILES
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Adenosine Triphosphate ◽  
Thiol Groups

scholarly journals The amino acid sequence of the peptide containing the thiol group of creatine kinase from normal and dystrophic chicken breast muscle. Comparison of some of the immunological properties of the antibodies developed in rabbits against these enzymes

1974 ◽  
Vol 143 (1) ◽  
pp. 171-179 ◽  
Author(s):  
Buddha P. Roy
Keyword(s):  
Creatine Kinase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
Chicken Breast ◽  
Thiol Groups ◽  
Dystrophic Muscle ◽  
Muscle Enzymes ◽  
Chicken Muscle ◽  
Dystrophic Chicken

The major14C-labelled peptides from creatine kinase from normal and dystrophic chicken muscle obtained by carboxymethylating the reactive thiol groups with iodo[2-14C]acetic acid and digestion with trypsin were purified by ion-exchange chromatography on Dowex-50 (X2) and by paper electrophoresis. The chromatographic characteristics of the14C-labelled peptides, their electrophoretic mobilities at pH6.5, and their amino acid compositions were identical for the two enzymes. The sequence of amino acids around the essential thiol groups of creatine kinase from normal and dystrophic chicken muscle was shown to be Ile-Leu-Thr-CmCys-Pro-Ser-Asn-Leu-Gly-Thr-Gly-Leu-Arg (CmCys, carboxymethylcysteine). This sequence is almost identical with that for the creatine kinases in human and ox muscle and bovine brain and is very similar to that of arginine kinase from lobster muscle. Antibodies to the enzymes were raised in rabbits and their reaction with the creatine kinase from normal and dystrophic muscles in interfacial, immunodiffusion and immunoelectrophoretic experiments was studied. The cross-reaction between normal muscle creatine kinase and antisera against the dystrophic muscle enzyme (or vice versa) observed by immunodiffusion and by immunoelectrophoretic experiments further suggests that the enzymes from normal and dystrophic chicken muscle are similar in structure. The results of the present study, the identical amino acid sequence of the peptides containing the reactive thiol group from both the normal and dystrophic chicken muscle enzymes and the immunological similarities of the two enzymes are in accord with the similarity of the two enzymes observed by Roy et al. (1970).

scholarly journals Bovine brain creatine phosphotransferase: amino acid sequence around the essential thiol groups

1970 ◽  
Vol 117 (2) ◽  
pp. 30P-31P ◽  
Author(s):  
R S Atherton ◽  
J F Laws ◽  
B J Miles ◽  
A R Thomson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bovine Brain ◽  
Thiol Groups

scholarly journals Cloning and expression of a new mammalian chaperonin gene from a multipotent hematopoietic progenitor clone

Blood ◽  
1994 ◽  
Vol 84 (7) ◽  
pp. 2171-2174
Author(s):  
X Xie ◽  
R Palacios
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Library ◽  
Adenosine Triphosphate ◽  
Molecular Chaperones ◽  
Amino Acid Sequence Identity ◽  
Cloning And Expression ◽  
Hematopoietic Progenitor ◽  
Sequence Identity ◽  
T Complex

Molecular chaperones assist in the folding and assembly of proteins in cells. Although chaperonins have been shown in prokaryotes, mitochondria, and chloroplasts long-ago, a cytoplasmic heteromeric chaperonin complex was isolated only recently and found to contain at least five to six polypeptides, one of which was identified as the product of the T complex polypeptide-1 (TCP-1) gene. We have isolated and cloned a novel gene called A45 from a cDNA library constructed from poly (A)+ RNA of a multipotent hematopoietic progenitor clone. The A45 cDNA encodes a predicted polypeptide of M(r) 58,118 that exhibits 32% overall amino acid sequence identity to TCP-1 and contains the putative adenosine triphosphate-binding domain and two characteristic consensus regions that are conserved in all chaperonins. The A45 gene is expressed in hematopoietic precursors cells at a much higher level than in nonhematopoietic cells and tissues. We conclude that A45 represents a new member of the mammalian chaperonins that is involved in the folding and assembly of polypeptides.

scholarly journals Cloning and expression of a new mammalian chaperonin gene from a multipotent hematopoietic progenitor clone

Blood ◽  
1994 ◽  
Vol 84 (7) ◽  
pp. 2171-2174 ◽  
Author(s):  
X Xie ◽  
R Palacios
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cdna Library ◽  
Adenosine Triphosphate ◽  
Molecular Chaperones ◽  
Amino Acid Sequence Identity ◽  
Cloning And Expression ◽  
Hematopoietic Progenitor ◽  
Sequence Identity ◽  
T Complex

Abstract Molecular chaperones assist in the folding and assembly of proteins in cells. Although chaperonins have been shown in prokaryotes, mitochondria, and chloroplasts long-ago, a cytoplasmic heteromeric chaperonin complex was isolated only recently and found to contain at least five to six polypeptides, one of which was identified as the product of the T complex polypeptide-1 (TCP-1) gene. We have isolated and cloned a novel gene called A45 from a cDNA library constructed from poly (A)+ RNA of a multipotent hematopoietic progenitor clone. The A45 cDNA encodes a predicted polypeptide of M(r) 58,118 that exhibits 32% overall amino acid sequence identity to TCP-1 and contains the putative adenosine triphosphate-binding domain and two characteristic consensus regions that are conserved in all chaperonins. The A45 gene is expressed in hematopoietic precursors cells at a much higher level than in nonhematopoietic cells and tissues. We conclude that A45 represents a new member of the mammalian chaperonins that is involved in the folding and assembly of polypeptides.

Studies on adenosine triphosphate transphosphorylases. Amino acid sequence of rabbit muscle ATP-AMP transphosphorylase

Biochemistry ◽  
1984 ◽  
Vol 23 (11) ◽  
pp. 2393-2399 ◽  
Author(s):  
Stephen A. Kuby ◽  
Richard H. Palmieri ◽  
Asta Frischat ◽  
Anne H. Fischer ◽  
Lily H. Wu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Adenosine Triphosphate ◽  
Rabbit Muscle

scholarly journals The amino acid sequence of rabbit muscle triose phosphate isomerase

1975 ◽  
Vol 145 (2) ◽  
pp. 335-344 ◽  
Author(s):  
P H Corran ◽  
S G Waley
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Triose Phosphate Isomerase ◽  
British Library ◽  
Rabbit Muscle ◽  
Amino Acid Residues ◽  
Thiol Groups ◽  
Muscle Enzyme ◽  
Triose Phosphate ◽  
Lending Library

The amino acid sequence of rabbit muscle triose phosphate isomerase was deduced by characterizing peptides that overlap the tryptic peptides. Thiol groups were modified by oxidation, carboxymethylation or aminoen. About 50 peptides that provided information about overlaps were isolated; the peptides were mostly characterized by their compositions and N-terminal residues. The peptide chains contain 248 amino acid residues, and no evidence for dissimilarity of the two subunits that comprise the native enzyme was found. The sequence of the rabbit muscle enzyme may be compared with that of the coelacanth enzyme (Kolb et al., 1974): 84% of the residues are in identical positions. Similarly, comparison of the sequence with that inferred for the chicken enzyme (Furth et al., 1974) shows that 87% of the residues are in identical positions. Limited though these comparisons are, they suggest that triose phosphate isomerase has one of the lowest rates of evolutionary change. An extended version of the present paper has been deposited as Supplementary Publication SUP 50040 (42 pages) at the British Library (Lending Division) (formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms given in Biochem. J. (1975) 145, 5.

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.

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