The amino acid sequence of chymopapain from Carica papaya

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.

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Amino acid sequence of cyanogen bromide fragment CB5 of human hemopexin

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19890803 ◽

1989 ◽

Vol 54 (3) ◽

pp. 803-810 ◽

Cited By ~ 1

Author(s):

Ivan Kluh ◽

Ladislav Morávek ◽

Manfred Pavlík

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Acid Hydrolysis ◽

Cyanogen Bromide ◽

Polypeptide Chain ◽

Amino Acid Residues ◽

Mild Acid Hydrolysis ◽

Methionine Residue ◽

Cyanogen Bromide Fragment ◽

Mild Acid

Cyanogen bromide fragment CB5 represents the region of the polypeptide chain of hemopexin between the fourth and fifth methionine residue (residues 232-352). It contains 120 amino acid residues in the following sequence: Arg-Cys-Ser-Pro-His-Leu-Val-Leu-Ser-Ala-Leu-Thr-Ser-Asp-Asn-His-Gly-Ala-Thr-Tyr-Ala-Phe-Ser-Gly-Thr-His-Tyr-Trp-Arg-Leu-Asp-Thr-Ser-Arg-Asp-Gly-Trp-His-Ser-Trp-Pro-Ile-Ala-His-Gln-Trp-Pro-Gln-Gly-Pro-Ser-Ala-Val-Asp-Ala-Ala-Phe-Ser-Trp-Glu-Glu-Lys-Leu-Tyr-Leu-Val-Gln-Gly-Thr-Gln-Val-Tyr-Val-Phe-Leu-Thr-Lys-Gly-Gly-Tyr-Thr-Leu-Val-Ser-Gly-Tyr-Pro-Lys-Arg-Leu-Glu-Lys-Glu-Val-Gly-Thr-Pro-His-Gly-Ile-Ile-Leu-Asp-Ser-Val-Asp-Ala-Ala-Phe-Ile-Cys-Pro-Gly-Ser-Ser-Arg-Leu-His-Ile-Met. The sequence was derived from the data on peptides prepared by cleavage of fragment CB5 by mild acid hydrolysis, by trypsin and chymotrypsin.

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Primary structure of the major β-chain of rat haemoglobins

Biochemical Journal ◽

10.1042/bj1730321 ◽

1978 ◽

Vol 173 (1) ◽

pp. 321-330 ◽

Cited By ~ 37

Author(s):

Laura M. Garrick ◽

Richard L. Sloan ◽

Thomas W. Ryan ◽

Thomas J. Klonowski ◽

Michael D. Garrick

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Allelic Variation ◽

Peptide Sequencing ◽

Exchange Chromatography ◽

British Library ◽

Individual Sequences ◽

Lysine Residues ◽

Cnbr Cleavage ◽

Β Chain

The amino acid sequence of the major β-chain, IIβ, from rat haemoglobins was established with an automated sequencer. Amino acid heterogeneities were found that appear to result from allelic variation at particular residues. We applied several new or unusual techniques in determining the sequence: (1) reaction of the polypeptide with dansylaziridine for detection of cysteine; (2) blockage of the N-terminal residue and the ε-amino group of lysine residues with 1-fluoro-2-nitro-4-trimethylammoniobenzene iodide and subsequent identification of the modified lysine phenylthiohydantoin by absorbance at 420nm; (3) identification of histidine phenylthiohydantoin by its blue fluorescence under long-wave u.v. light; (4) cleavage of the chain into two or three fragments and subsequent sequencing without purification [a detailed statement giving the major phenylthiohydantoins assigned at each step for each sequence run before their alignment in individual sequences has been deposited as Supplementary Publication SUP 50084 (10 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5]; (5) separation of fragments produced by CNBr cleavage by cation-exchange chromatography; (6) peptide sequencing after attachment of the peptide to cytochrome c. The amino acid sequence was confirmed by amino acid compositions of the complete chain, of CNBr fragments 1 and 3, and of 11 purified tryptic peptides.

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The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena

Biochemical Journal ◽

10.1042/bj1450353 ◽

1975 ◽

Vol 145 (2) ◽

pp. 353-360 ◽

Cited By ~ 26

Author(s):

S Sato ◽

T Uchida

Keyword(s):

Biological Activity ◽

Amino Acid ◽

Amino Acid Sequence ◽

Crucial Role ◽

Science And Technology ◽

British Library ◽

Amino Acid Residues ◽

Complete Amino Acid Sequence ◽

Lending Library

1. RNAase (ribonuclease) U2, a purine-specific RNAase, was reduced, aminoethylated and hydrolysed with trypsin, chymotrypsin and thermolysin. On the basis of the analyses of the resulting peptides, the complete amino acid sequence of RNAase U2 was determined, 2. When the sequence was compared with the amino acid sequence of RNAase T1 (EC 3.1.4.8), the following regions were found to be similar in the two enzymes; Tyr-Pro-His-Gln-Tyr (38-42) in RNAase U2 and Tyr-Pro-His-Lys-Tyr (38-42) in RNAase T1, Glu-Phe-Pro-Leu-Val (61-65) in RNAase U2 and Glu-Trp-Pro-Ile-Leu (58-62) in RNAase T1, Asp-Arg-Val-Ile-Tyr-Gln (83-88) in RNAase U2 and Asp-Arg-Val-Phe-Asn (76-81) in RNAase T1 and Val-Thr-His-Thr-Gly-Ala (98-103) in RNAase U2 and Ile-Thr-His-Thr-Gly-Ala (90-95) in RNAase T1. All of the amino acid residues, histidine-40, glutamate-58, arginine-77 and histidine-92, which were found to play a crucial role in the biological activity of RNAase T1, were included in the regions cited here. 3. Detailed evidence for the amino acid sequence of the sequence of the proteins has been deposited as Supplementary Publication SUP 50041 (33 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 indicated in Biochem. J. (1975), 145, 5.

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

Biochemical Journal ◽

10.1042/bj1990211 ◽

1981 ◽

Vol 199 (1) ◽

pp. 211-218 ◽

Cited By ~ 27

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.

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

Biochemical Journal ◽

10.1042/bj1240061 ◽

1971 ◽

Vol 124 (1) ◽

pp. 61-67 ◽

Cited By ~ 11

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.

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The amino acid sequence of troponin I from rabbit skeletal muscle

Biochemical Journal ◽

10.1042/bj1490493 ◽

1975 ◽

Vol 149 (2) ◽

pp. 493-496 ◽

Cited By ~ 71

Author(s):

J M Wilkinson ◽

R J A. Grand

Keyword(s):

Skeletal Muscle ◽

Molecular Weight ◽

Amino Acid ◽

Amino Acid Sequence ◽

Cyanogen Bromide ◽

Troponin I ◽

Rabbit Skeletal Muscle ◽

British Library ◽

Amino Acid Residues ◽

N Terminus

The complete amino acid sequence of rabbit skeletal muscle troponin I was determined by the isolation of the cyanogen bromide fragments and the tryptic methionine-containing peptides. Troponin I contains 179 amino acid residues and has a molecular weight of 20864. Its N-terminus is acetylated. Detailed evidence on which the sequence is based has been deposited as Supplementary Publication SUP 50055 (23 pages) at the British Library (Lending Division), Boston Spa, Wetherby, West Yorkshire LS23 7QB, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.

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Neurotoxins from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides

Biochemical Journal ◽

10.1042/bj2130031 ◽

1983 ◽

Vol 213 (1) ◽

pp. 31-38 ◽

Cited By ~ 11

Author(s):

N Tamiya ◽

N Maeda ◽

H G Cogger

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Paper Electrophoresis ◽

Amino Acid Sequences ◽

British Library ◽

Amino Acid Residues ◽

Protein Amino Acid ◽

Tryptic Peptides ◽

Sea Snakes ◽

And Migration

The main neurotoxic components, toxins Hydrophis ornatus a and Hydrophis lapemoides a, were isolated from the venoms of the sea snakes Hydrophis ornatus and Hydrophis lapemoides respectively. The amino acid sequence of toxin Hydrophis ornatus a was deduced to be identical with that of toxin Astrotia stokesii a [Maeda & Tamiya (1978) Biochem. J. 175, 507-517] on the basis of identity of the tryptic peptide ‘map’ and the amino acid composition of each peptide. The amino acid sequence of toxin Hydrophis lapemoides a was determined mainly on the basis of identity of the amino acid compositions, mobilities on paper electrophoresis and migration positions on paper chromatography of the tryptic peptides with those of other sea-snake toxins whose sequences are known. Both toxins Hydrophis ornatus a and Hydrophis lapemoides a consisted of 60 amino acid residues and there were six amino acid replacements between them. The taxonomy of sea snakes in the Hydrophis ornatus complex has long been confused, and the above snakes were originally assigned to taxa that proved to be inconsistent with the relationships indicated by the neurotoxin amino acid sequences obtained. A subsequent re-examination of the specimens revealed an error in the original identifications and demonstrated the value of the protein amino acid sequences in systematic and phylogenetic studies. The isolation procedure and results of amino acid analysis of the tryptic peptides have been deposited as Supplementary Publication SUP 50121 (8 pages) with the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1983) 209, 5.

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

Biochemical Journal ◽

10.1042/bj2660221 ◽

1990 ◽

Vol 266 (1) ◽

pp. 221-225 ◽

Cited By ~ 22

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.

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The amino acid sequence of rabbit muscle triose phosphate isomerase

Biochemical Journal ◽

10.1042/bj1450335 ◽

1975 ◽

Vol 145 (2) ◽

pp. 335-344 ◽

Cited By ~ 50

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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Amino acid sequence of the smaller basic protein from rat brain myelin

Biochemical Journal ◽

10.1042/bj1410243 ◽

1974 ◽

Vol 141 (1) ◽

pp. 243-255 ◽

Cited By ~ 130

Author(s):

Peter R. Dunkley ◽

Patrick R. Carnegie

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Rat Brain ◽

Basic Protein ◽

Detailed Comparison ◽

British Library ◽

Amino Acid Residues ◽

Variable Regions ◽

Basic Proteins ◽

Lending Library

1. The complete amino acid sequence of the smaller basic protein from rat brain myelin was determined. This protein differs from myelin basic proteins of other species in having a deletion of a polypeptide of 40 amino acid residues from the centre of the molecule. 2. A detailed comparison is made of the constant and variable regions in a group of myelin basic proteins from six species. 3. An arginine residue in the rat protein was found to be partially methylated. The ratio of methylated to unmethylated arginine at this position differed from that found for the human basic protein. 4. Three tryptic peptides were isolated in more than one form. The differences between the two forms of each peptide are discussed in relation to the electrophoretic heterogeneity of myelin basic proteins, which is known to occur at alkaline pH values. 5. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50029 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.

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