The Enzymic Digestion of Cod Tropomyosin

1962 ◽  
Vol 19 (6) ◽  
pp. 1095-1104
Author(s):  
B. Truscott ◽  
P. L. Hoogland ◽  
P. H. Odense ◽  
A. E. Waddell
Keyword(s):  
Amino Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Performic Acid ◽  
Amino Acid Residues ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Enzymic Digestion ◽  
Disulphide Bonds ◽  
Terminal Amino

Tropomyosin from cod muscle can be oxidized with performic acid to cleave disulphide bonds without degradation of other amino acid residues. The ε-amino groups of lysine within the molecule can be substituted readily with carbobenzoxy-groups for protection against digestion by trypsin. The digestions by trypsin of carbobenzoxy-substituted tropomyosin, and by chymotrypsin of oxidized tropomyosin, have been shown to be reproducible, providing peptides suitable for amino acid sequence studies. The peptides so obtained were separated by ion-exchange chromatography using a Beckman/Spinco Amino Acid Analyzer.After treatment with urea, cod tropomyosin does not yield a free N-terminal amino acid as has been reported for rabbit tropomyosin.

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 Tamm–Horsfall urinary glycoprotein. The chemical composition

1970 ◽  
Vol 120 (2) ◽  
pp. 417-424 ◽  
Author(s):  
A. P. Fletcher ◽  
A. Neuberger ◽  
Wendy A. Ratcliffe
Keyword(s):  
Amino Acid ◽  
Performic Acid ◽  
Acid Oxidation ◽  
Amino Acid Residues ◽  
Carbohydrate Composition ◽  
Thiol Groups ◽  
Terminal Amino Acid ◽  
Cystine Content ◽  
Terminal Amino ◽  
Urinary Glycoprotein

1. A revised amino acid and carbohydrate composition of human Tamm–Horsfall glycoprotein is presented. 2. No significant differences were obtained in the amino acid composition of Tamm–Horsfall glycoprotein isolated from patients with cystic fibrosis. 3. The glycoprotein was shown to possess a high half-cystine content of 1 per 11–12 amino acid residues, which has been confirmed by performic acid oxidation and S-alkylation with iodoacetate and iodoacetamide. No thiol groups were detected in the glycoprotein. 4. Treatment of the glycoprotein with 0.5m-sodium hydroxide at 4°C for 2 days did not release heterosaccharide material, which suggests that the predominant carbohydrate–protein linkages present are not of the O-glycosidic type. 5. No N-terminal amino acid was detected in the glycoprotein.

scholarly journals Isolation and a partial amino acid sequence of insulin from the islet tissue of cod (Gadus callarias)

1968 ◽  
Vol 106 (2) ◽  
pp. 531-541 ◽  
Author(s):  
P T Grant ◽  
K. B. M. Reid
Keyword(s):  
Amino Acid ◽  
Ion Exchange ◽  
Gel Filtration ◽  
Bovine Insulin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Performic Acid ◽  
Amino Acid Residues ◽  
Islet Tissue ◽  
A Chain

1. Insulin has been isolated by gel filtration and ion-exchange chromatography from extracts of the discrete islet tissue of cod. The final preparation yielded a single band on electrophoresis at two pH values. The biological potency was 11·5 international units/mg. in mouse-convulsion and other assay procedures. 2. Glycine and methionine were shown to be the N-terminal amino acids of the A and B chains respectively. An estimate of the molecular weight together with amino acid analyses indicated that cod insulin, like the bovine hormone, consists of 51 amino acid residues. In contrast, the amino acid composition differs markedly from bovine insulin. 3. Oxidation of insulin with performic acid yielded the A and B peptide chains, which were separated by ion-exchange chromatography. Sequence studies on smaller peptides isolated from enzymic digests or from dilute acetic acid hydrolysates of the two chains have established the sequential order of 14 of the 21 amino acid residues of the A chain and 25 of the 30 amino acid residues of the B chain.

Thermolytic digest of chicken pepsin

1981 ◽  
Vol 46 (8) ◽  
pp. 1994-2004 ◽  
Author(s):  
Miroslav Baudyš ◽  
Vladimír Kostka ◽  
Helena Keilová
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Linear Structure ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence ◽  
High Voltage Electrophoresis ◽  
Final Purification

Chicken pepsin prepared by the activation of pepsinogen was digested with thermolysin. The thermolytic digest was fractionated by chromatography on Sephadex G-25 fine. Certain fractions were subsequently subjected to ion exchange chromatography on Dowex 50-X2. The final purification was effected by paper chromatography and high voltage electrophoresis. By these procedures a series of homogeneous peptides was obtained; of the latter 54 nonoverlapping (save for a few exceptions) peptides are described in this paper. These peptides in addition to the thermolytic peptides reported before represent 80% of the linear structure of the whole molecule. The N-terminal amino acid sequence of chicken pepsin is discussed from the viewpoint of the recent data obtained by the analysis of the thermolytic digest.

scholarly journals Deletion of the Actin-Associated Tropomyosin Tpm3 Leads to Reduced Cell Complexity in Cultured Hippocampal Neurons—New Insights into the Role of the C-Terminal Region of Tpm3.1

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 715
Author(s):  
Tamara Tomanić ◽  
Claire Martin ◽  
Holly Stefen ◽  
Esmeralda Parić ◽  
Peter Gunning ◽  
...  
Keyword(s):  
Amino Acid ◽  
Hippocampal Neurons ◽  
Molecular Mechanisms ◽  
Growth Cones ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
C Terminus ◽  
Primary Mouse ◽  
Terminal Amino

Tropomyosins (Tpms) have been described as master regulators of actin, with Tpm3 products shown to be involved in early developmental processes, and the Tpm3 isoform Tpm3.1 controlling changes in the size of neuronal growth cones and neurite growth. Here, we used primary mouse hippocampal neurons of C57/Bl6 wild type and Bl6Tpm3flox transgenic mice to carry out morphometric analyses in response to the absence of Tpm3 products, as well as to investigate the effect of C-terminal truncation on the ability of Tpm3.1 to modulate neuronal morphogenesis. We found that the knock-out of Tpm3 leads to decreased neurite length and complexity, and that the deletion of two amino acid residues at the C-terminus of Tpm3.1 leads to more detrimental changes in neurite morphology than the deletion of six amino acid residues. We also found that Tpm3.1 that lacks the 6 C-terminal amino acid residues does not associate with stress fibres, does not segregate to the tips of neurites, and does not impact the amount of the filamentous actin pool at the axonal growth cones, as opposed to Tpm3.1, which lacks the two C-terminal amino acid residues. Our study provides further insight into the role of both Tpm3 products and the C-terminus of Tpm3.1, and it forms the basis for future studies that aim to identify the molecular mechanisms underlying Tpm3.1 targeting to different subcellular compartments.

Importance of Terminal Amino Acid Residues to the Transport of Oligopeptides across the Caco-2 Cell Monolayer

2017 ◽  
Vol 65 (35) ◽  
pp. 7705-7712 ◽  
Author(s):  
Long Ding ◽  
Liying Wang ◽  
Zhipeng Yu ◽  
Sitong Ma ◽  
Zhiyang Du ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Monolayer ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
Terminal Amino

scholarly journals Properties of Gluten Fractions Prepared by Ion-Exchange Chromatography on Carboxymethyl-Cellulose

1963 ◽  
Vol 16 (3) ◽  
pp. 717 ◽  
Author(s):  
JW Lee ◽  
MV Tracey ◽  
DJ Winzor ◽  
CW Wrigley ◽  
H Zentner
Keyword(s):  
Gel Electrophoresis ◽  
Wheat Gluten ◽  
Methyl Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Gel Technique ◽  
Reversible Association ◽  
Carboxy Methyl

Seven fractions obtained from wheat gluten by chromatography on carboxy~ methyl-cellulose were studied by ultracentrifugation, gel electrophoresis, chemical, and N-terminal amino acid analysis. On rechromatography, five fractions eluted by sodium chloride behaved as distinct entities. illtracentrifuge experiments indicated that four of these were each undergoing rapid, reversible association. Several N-terminal amino acids were found in each of the fractions which, moreover, could be resolved by the gel technique into a number of electrophoretic bands, some bands being common to those of neighbouring fractions. Total nitrogen values showed the chromatographic samples to be essentially free from non-protein material.

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