Tamm–Horsfall urinary glycoprotein. The chemical composition

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.

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The Enzymic Digestion of Cod Tropomyosin

Journal of the Fisheries Research Board of Canada ◽

10.1139/f62-072 ◽

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.

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Alterations of the carboxyl-terminal amino acid residues of Escherichia coli lipoprotein affect the formation of murein-bound lipoprotein.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)41811-x ◽

1992 ◽

Vol 267 (27) ◽

pp. 19560-19564

Author(s):

W.Y. Zhang ◽

H.C. Wu

Keyword(s):

Escherichia Coli ◽

Amino Acid ◽

Amino Acid Residues ◽

Terminal Amino Acid ◽

Terminal Amino ◽

Carboxyl Terminal

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The major kidney AE1 isoform does not bind ankyrin (Ank1) in vitro. An essential role for the 79 NH2-terminal amino acid residues of band 3.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)31621-1 ◽

1994 ◽

Vol 269 (51) ◽

pp. 32201-32208

Author(s):

Y. Ding ◽

J.R. Casey ◽

R.R. Kopito

Keyword(s):

Amino Acid ◽

Essential Role ◽

Band 3 ◽

Amino Acid Residues ◽

Terminal Amino Acid ◽

Terminal Amino

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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 ◽

10.3390/cells10030715 ◽

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.

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