scholarly journals Amino acid sequences around the cysteine residues of rabbit muscle triose phosphate isomerase

1971 ◽  
Vol 122 (2) ◽  
pp. 209-218 ◽  
Author(s):  
Janet C. Miller ◽  
S. G. Waley
Keyword(s):  
Amino Acid ◽  
Cyanogen Bromide ◽  
Triose Phosphate Isomerase ◽  
Amino Acid Sequences ◽  
Cysteine Residues ◽  
Rabbit Muscle ◽  
Amino Acid Residues ◽  
Triose Phosphate ◽  
Methionine Residues ◽  
Polypeptide Chains

1. The nature of the subunits in rabbit muscle triose phosphate isomerase has been investigated. 2. Amino acid analyses show that there are five cysteine residues and two methionine residues/subunit. 3. The amino acid sequences around the cysteine residues have been determined; these account for about 75 residues. 4. Cleavage at the methionine residues with cyanogen bromide gave three fragments. 5. These results show that the subunits correspond to polypeptide chains, containing about 230 amino acid residues. The chains in triose phosphate isomerase seem to be shorter than those of other glycolytic enzymes.

scholarly journals The tryptic peptides of rabbit muscle triose phosphate isomerase

1974 ◽  
Vol 139 (1) ◽  
pp. 1-10 ◽  
Author(s):  
P. H. Corran ◽  
S. G. Waley
Keyword(s):  
Gel Filtration ◽  
Paper Electrophoresis ◽  
Triose Phosphate Isomerase ◽  
British Library ◽  
Rabbit Muscle ◽  
Amino Acid Residues ◽  
Tryptic Peptides ◽  
Triose Phosphate ◽  
Lending Library ◽  
Polypeptide Chains

1. The peptides obtained by tryptic digestion of S-[14C]carboxymethylated rabbit muscle triose phosphate isomerase have been studied. 2. The first step in the fractionation of the tryptic digest was gel filtration on coupled columns of Sephadex G-25 and G-50. Further fractionation was carried out by paper electrophoresis and paper chromatography. 3. The digest contained 26 peptides and three free amino acids. The sizes of the peptides ranged from two to 29 residues. 4. The sequences of the peptides have been determined. 5. The length of the polypeptide chains is about 250 amino acid residues. 6. The variant sequences encountered were due to partial deamidation; this may be one of the reasons for multiple forms of the enzyme. 7. The chicken and rabbit enzymes are compared. 8. Detailed evidence for the sequences of the tryptic peptides has been deposited as Supplementary Publication SUP 50024 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. (1973) 131, 5.

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.

Cloning and sequencing of two genes encoding chitinases A and B from Bacillus cereus CH

2001 ◽  
Vol 47 (10) ◽  
pp. 895-902 ◽  
Author(s):  
Naoto Mabuchi ◽  
Yoshio Araki
Keyword(s):  
Amino Acid ◽  
Bacillus Cereus ◽  
Catalytic Domain ◽  
Amino Acid Sequences ◽  
Open Reading Frames ◽  
Amino Acid Residues ◽  
Chitinase A ◽  
Genes Encoding ◽  
Fibronectin Type Iii ◽  
Polypeptide Chains

Two genes encoding chitinases A and B (chiA and chiB) from Bacillus cereus CH were cloned into Escherichia coli XL1-Blue MRF' by using pBluescript II SK+, and their nucleotide sequences were determined. Open reading frames of the chiA and chiB genes encoded distinct polypeptide chains consisting of 360 and 674 amino acid residues, respectively, with calculated molecular sizes of 39 470 and 74 261 Da, respectively. Comparison of the deduced amino acid sequences with those of other bacterial chitinases revealed that chitinase A consisted of a catalytic domain, while chitinase B consisted of three functional domains, a catalytic domain, a fibronectin type III-like domain, and a cellulose-binding domain. The primary structures of these two proteins were not similar to each other.Key words: Bacillus cereus, chitinase, cloning.

scholarly journals Studies on the subunit structure and amino acid sequence of triose phosphate isomerase from chicken breast muscle

1974 ◽  
Vol 139 (1) ◽  
pp. 11-22 ◽  
Author(s):  
Anna J. Furth ◽  
J. D. Milman ◽  
J. D. Priddle ◽  
R. E. Offord
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Triose Phosphate Isomerase ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Rabbit Muscle ◽  
Tryptic Peptides ◽  
Amino Acid Compositions ◽  
Triose Phosphate

1. Triose phosphate isomerase was prepared by chromatography on DEAE-cellulose of an (NH4)2SO4 fraction of an extract of homogenized chicken breast muscle. The product is homogeneous on gel electrophoresis and is suitable for growing crystals for X-ray work. The specific activity is 10000 units/mg and the value for E0.1%280 is 1.20. 2. Comparison between the sum of the amino acid compositions of the tryptic peptides of the protein and the amino acid composition obtained on total hydrolysis of the protein indicates that the relative subunit mass is about 27000. 3. These data, together with the results of the examination of the amino acid compositions of a number of minor peptides, the number of peptides in the tryptic digest and the complete amino acid sequences of the tryptic peptides (the determination of which is described here), give no indication that the subunits are dissimilar. 4. A tentative amino acid sequence is presented for the protein, in which the ordering of the tryptic peptides is derived by homology with the sequence of the rabbit muscle enzyme (Corran & Waley, 1973). 5. An appendix describes the use that was made of mass spectrometry in the determination of some of the sequences. Mass-spectrometric data have been obtained for 35 residues, that is about 15% of the total sequence of the protein. 6. An extended version of the present paper has been deposited as Supplementary Publication SUP 50025 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 may be obtained on the terms given in Biochem. J. (1973) 131, 5.

scholarly journals Two globin strains in the giant annelid extracellular haemoglobins

1987 ◽  
Vol 241 (2) ◽  
pp. 441-445 ◽  
Author(s):  
T Gotoh ◽  
F Shishikura ◽  
J W Snow ◽  
K I Ereifej ◽  
S N Vinogradov ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lumbricus Terrestris ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Reverse Phase ◽  
Terminal Amino ◽  
Polypeptide Chains

The constituent polypeptide chains I, II, III and IV of the giant extracellular haemoglobin of the oligochaete Lumbricus terrestris were isolated by mono Q ion-exchange chromatography and C8 reverse-phase chromatography. The N-terminal amino acid sequences of Lumbricus chains I, III and IV were determined and aligned with those of Lumbricus chain II and the four chains of the extracellular haemoglobin of the polychaete Tylorrhynchus heterochaetus. Three invariant amino acid residues, Cys-7, Val-15 and Trp-19, were found to occur in the N-terminal segments (17-22 residues) of the eight chains of Lumbricus and Tylorrhynchus haemoglobins. In addition, it was found that the eight sequences could be separated into two groups: ‘A’, consisting of Lumbricus chains I and II and Tylorrhynchus chains I and IIA, having invariant Lys-14 and Lys-16, and ‘B’, consisting of Lumbricus chains III and IV and Tylorrhynchus IIB and IIC, having invariant Cys-6, Ser-8 and Asp-11. This result suggests that there are two strains of globin chain in the annelid extracellular haemoglobins.

scholarly journals Studies On Reduced Wool Ix. The N-Terminal Sequence of A Fragment Produced by Cleavage of Component 8 With Cyanogen Bromide

1969 ◽  
Vol 22 (2) ◽  
pp. 471 ◽  
Author(s):  
IJ O'donnell
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cyanogen Bromide ◽  
Amino Acid Sequences ◽  
Chemical Environment ◽  
Terminal Sequence ◽  
Terminal Residue ◽  
Amino Terminal ◽  
Fundamental Sequence ◽  
Methionine Residues

Component 8 is a major component extracted from reduced and carboxy-methylated wool. Further study of its reaction with cyanogen bromide and of the fractions obtained under carefully controlled disaggregating conditions has rev<\laled that while most of the methionine residues are in the same position relative to the ends of the chains, at least 30% of them appear to be in a different chemical environment from the rest. The evidence can be interpreted in terms of variations in some of the amino acids at particular points in a fundamental sequence of the 60 residues (CNBr3) at the amino terminal end. Further amino acid sequences near the acetylated terminal residue have been determined and provide examples of the amino acid variatioIl along the chain. One sequeIlce with variants is: N-acetyISer-(Tyr or Phe Or Pro)-Asp-(Phe or Leu)-SCMCySH-Leu-Pro-Asp-Leu-Ser-Phe-Arg-. There is a region in component 8 where many of the S-carboxymethylcysteine residues are congregated.

scholarly journals Primary structure of a constituent polypeptide chain (AIII) of the giant haemoglobin from the deep-sea tube worm Lamellibrachia. A possible H2S-binding site

1990 ◽  
Vol 266 (1) ◽  
pp. 221-225 ◽  
Author(s):  
T Suzuki ◽  
T Takagi ◽  
S Ohta
Keyword(s):  
Amino Acid ◽  
Deep Sea ◽  
Thiol Group ◽  
Cysteine Residue ◽  
Amino Acid Sequences ◽  
Intact Protein ◽  
Cysteine Residues ◽  
British Library ◽  
Amino Acid Residues ◽  
The Family

The deep-sea tube worm Lamellibrachia, belonging to the Phylum Vestimentifera, contains two giant extracellular haemoglobins, a 3000 kDa haemoglobin and a 440 kDa haemoglobin. The former consists of four haem-containing chains (AI-AIV) and two linker chains (AV and AVI) for the assembly of the haem-containing chains [Suzuki, Takagi & Ohta (1988) Biochem. J. 255, 541-545]. The tube-worm haemoglobins are believed to have a function of transporting sulphide (H2S) to internal bacterial symbionts, as well as of facilitating O2 transport [Arp & Childress (1983) Science 219, 295-297]. We have determined the complete amino acid sequence of Lamellibrachia chain AIII by automated or manual Edman sequencing. The chain is composed of 144 amino acid residues, has three cysteine residues at positions 3, 74 and 133, and has a molecular mass of 16,620 Da, including a haem group. The sequence showed significant homology (30-50% identity) with those of haem-containing chains of annelid giant haemoglobins. Two of the three cysteine residues are located at the positions where an intrachain disulphide bridge is formed in all annelid chains, but the remaining one (Cys-74) was located at a unique position, compared with annelid chains. Since the chain AIII was shown to have a reactive thiol group in the intact 3000 kDa molecule by preliminary experiments, the cysteine residue at position 74 appears to be one of the most probable candidates for the sulphide-binding sites. A phylogenetic tree was constructed from nine chains of annelid giant haemoglobins and one chain of vestimentiferan tube-worm haemoglobin now determined. The tree clearly showed that Lamellibrachia chain AIII belongs to the family of strain A of annelid giant haemoglobins, and that the two classes of Annelida, polychaete and oligochaete, and the vestimentiferan tube worm diverged at almost the same time. H.p.l.c. patterns of peptides (Figs. 4-7), amino acid compositions of peptides (Table 2) and amino acid sequences of intact protein and peptides (Table 3) have been deposited as Supplementary Publication SUP 50154 (13 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1990) 265, 5.

scholarly journals Amino Acid Sequence Studies on Sheep Liver Fructose-bisphosphatase. II The Complete Sequence

1983 ◽  
Vol 36 (3) ◽  
pp. 235 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Fructose Bisphosphatase ◽  
Proteolytic Digestion ◽  
Sheep Liver ◽  
Methionine Residues

The cyanogen bromide fragments of S-carboxymethylated fructose-bisphosphatase were purified. The amino acid sequences of the small fragments were determined by the dansyl-Edman method. The large fragments were subjected to proteolytic digestion to give smaller peptides more amenable for purification and sequencing by similar methods. Enzyme digests of the S-carboxymethylated enzyme gave overlap peptides containing the methionine residues.

scholarly journals Triose phosphate isomerase from the coelacanth. An approach to the rapid determination of an amino acid sequence with small amounts of material

1974 ◽  
Vol 137 (2) ◽  
pp. 185-197 ◽  
Author(s):  
Edith Kolb ◽  
J. Ieuan Harris ◽  
John Bridgen
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rapid Determination ◽  
Triose Phosphate Isomerase ◽  
Intact Protein ◽  
Sequence Information ◽  
Rabbit Muscle ◽  
Muscle Enzyme ◽  
Triose Phosphate

The preparation and purification of cyanogen bromide fragments from [14C]carboxymethylated coelacanth triose phosphate isomerase is presented. The automated sequencing of these fragments, the lysine-blocked tryptic peptides derived from them, and also of the intact protein, is described. Combination with results from manual sequence analysis has given the 247-residue amino acid sequence of coelacanth triose phosphate isomerase in 4 months, by using 100mg of enzyme. (Two small adjacent peptides were placed by homology with the rabbit enzyme.) Comparison of this sequence with that of the rabbit muscle enzyme shows that 207 (84%) of the residues are identical. This slow rate of evolutionary change (corresponding to two amino acid substitutions per 100 residues per 100 million years) is similar to that found for glyceraldehyde 3-phosphate dehydrogenase. The reliability of sequence information obtained by automated methods is discussed.

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