scholarly journals Brain adenosine 5′-triphosphate–creatine phosphotransferase. Purification, thiol group reactivity and the amino acid sequence around the reactive thiol groups

1970 ◽  
Vol 120 (3) ◽  
pp. 589-600 ◽  
Author(s):  
R. S. Atherton ◽  
J. F. Laws ◽  
B. J. Miles ◽  
A. R. Thomson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
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 The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275

1985 ◽  
Vol 229 (3) ◽  
pp. 791-797 ◽  
Author(s):  
R Bicknell ◽  
E L Emanuel ◽  
J Gagnon ◽  
S G Waley
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
The Other ◽  
Beta Lactamase ◽  
Beta Lactamases ◽  
Zinc Enzyme ◽  
Pseudomonas Maltophilia ◽  
Measurable Rate ◽  
Beta Lactamase Ii

The production and purification of a tetrameric zinc beta-lactamase from Pseudomonas maltophilia IID 1275 were greatly improved. Three charge variants were isolated by chromatofocusing. The subunits each contain two atomic proportions of zinc and (in two of the variants) one residue of cysteine. The thiol group is not required for activity, nor does it appear to bind to the metal. Replacement of zinc by cobalt, cadmium or nickel takes place at a measurable rate, and gives enzymes that are less active than the zinc enzyme. The properties of this enzyme differ from those of the other known zinc beta-lactamase, beta-lactamase II from Bacillus cereus. The amino acid sequence of the N-terminal 32 residues was determined; there is no similarity to the N-terminal sequences of other beta-lactamases.

scholarly journals The amino acid sequence and position of the free thiol group of a short-chain neurotoxin from common-death-adder (Acanthophis antarcticus) venom

1981 ◽  
Vol 199 (1) ◽  
pp. 211-218 ◽  
Author(s):  
H S Kim ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Lethal Dose ◽  
Thiol Group ◽  
Cysteine Residue ◽  
Short Chain ◽  
Amino Acid Residues ◽  
The Family ◽  
Free Thiol Group ◽  
The Common

The amino acid sequence of a short-chain neurotoxin Acanthophis antarcticus c (toxin Aa c) from the venom of an Australian elapid snake, the common death adder (Acanthophis antarcticus, subfamily Acanthophiinae) was elucidated. Toxin Aa c is composed of 62 amino acid residues, including eight half-cystine residues and a cysteine residue. The amino acid sequence of toxin Aa c is homologous with those of other short-chain neurotoxins found in snakes of the family Elapidae, especially with those from snakes of the subfamily Hydrophiinae. The single cysteine residue was located in position 4. Toxin Aa c has a lethal dose (LD50) of 0.08 micrograms/g body weight of mouse on intramuscular injection.

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 chymopapain from Carica papaya

1990 ◽  
Vol 266 (1) ◽  
pp. 75-81 ◽  
Author(s):  
D C Watson ◽  
M Yaguchi ◽  
K R Lynn
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Similarity ◽  
Thiol Group ◽  
Exchange Chromatography ◽  
British Library ◽  
Amino Acid Residues ◽  
Main Paper ◽  
Paper Supplement ◽  
Mild Acid

Chymopapain is a polypeptide of 218 amino acid residues. It has considerable structural similarity with papain and papaya proteinase omega, including conservation of the catalytic site and of the disulphide bonding. Chymopapain is like papaya proteinase omega in carrying four extra residues between papain positions 168 and 169, but differs from both papaya proteinases in the composition of its S2 subsite, as well as in having a second thiol group, Cys-117. Some evidence for the amino acid sequence of chymopapain has been deposited as Supplementary Publication SUP 50153 (12 pages) at the British Library Document Supply Centre, Boston Spa., Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1990) 265, 5. The information comprises Supplement Tables 1-4, which contain, in order, amino acid compositions of peptides from tryptic, peptic, CNBr and mild acid cleavages, Supplement Fig. 1, showing re-fractionation of selected peaks from Fig. 2 of the main paper. Supplement Fig. 2, showing cation-exchange chromatography of the earliest-eluted peak of Fig. 3 of the main paper, Supplement Fig. 3, showing reverse-phase h.p.l.c. of the later-eluted peak from Fig. 3 of the main paper, and Supplement Fig. 4, showing the separation of peptides after mild acid hydrolysis of CNBr-cleavage fragment CB3.

scholarly journals Amino acid sequences around the cysteine residue of calf lens α-crystallin

1971 ◽  
Vol 124 (1) ◽  
pp. 61-67 ◽  
Author(s):  
P. H. Corran ◽  
S. G. Waley
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Thiol Group ◽  
Cysteine Residue ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Radioactive Sodium ◽  
Group 2

1. Calf lens α-crystallin was carboxymethylated with radioactive sodium iodoacetate to label the thiol group. 2. The protein was then digested with trypsin or alternatively fractionated in urea to obtain the acidic (A) chains, which were then digested with trypsin. Either procedure gave two radioactive peptides containing carboxymethylcysteine. 3. These two peptides were closely related: the longer form contained 28 amino acid residues, and the shorter lacked two residues at the N-terminal end of the longer form. 4. The amino acid sequence of the peptides have been determined. 5. No evidence for the presence of more than one cysteine residue/chain was found. 6. The question of the molecular weight of the chains is discussed.

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 The subunit structure of rabbit skeletal-muscle phosphofructokinase and the amino acid sequence of the tryptic peptide containing the highly reactive thiol group

1977 ◽  
Vol 163 (2) ◽  
pp. 309-316 ◽  
Author(s):  
I A Simpson ◽  
M R Hollaway ◽  
J Beard
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tryptic Peptide ◽  
Peptide Mapping ◽  
Thiol Group ◽  
Cysteine Residue ◽  
Amino Acid Sequences ◽  
Class I ◽  
Subunit Structure

1. The single highly reactive (class I) thiol group per 80000-mol.wt. subunit of skeletal-muscle phosphofructokinase was specifically carboxymethylated with iodo[2-14C]acetate, and after denaturation the remaining thiol groups were carboxymethylated with bromo[2-3H]acetate. After tryptic digestion and peptide ‘mapping’ it was found that the 14C radioactivity was in a spot that did not contain significant amounts of 3H radioactivity, so it is concluded that there is not a second, ‘buried’ cysteine residue within a sequence identical with that of the class-I cysteine peptide. 2. The total number of tryptic peptides as well as the number of those containing cysteine, histidine or tryptophan were inconsistent with the smallest polypeptide chain of phosphofructokinase (mol.wt. about 80000) being composed of two identical amino acid sequences. 3. The amino acid sequence of the tryptic peptide containing the class-I thiol group was shown to be Cys-Lys-Asp-Phe-Arg. This sequence is compared with part of the sequence containing the highly reactive thiol group of phosphorylase.

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.

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