Gene expression and development : the third of five volumes constituting the proceedings of the 4th International Congress on Isozymes, held in Austin, Texas, June 14-19, 1982 / editors, Mario C. Rattazzi, John G. Scandalios, Gregory S. Whitt.
- International Congress on Isozymes
- Date:
- [cl983]
Licence: Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
Credit: Gene expression and development : the third of five volumes constituting the proceedings of the 4th International Congress on Isozymes, held in Austin, Texas, June 14-19, 1982 / editors, Mario C. Rattazzi, John G. Scandalios, Gregory S. Whitt. Source: Wellcome Collection.
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![Glycerol Phosphate Dehydrogenase Expression / 45 Drosophila Asn-Hi s-Pro-Glu-Hi s-Met-Gln-Asn-Leu-COOH gpdh''-i t-1 Sp-1 CPA Drosophila Asn-His-Pro-Glu-His-Met-COOH GPDH'^-S: T-1 Rabbit muscle Asn-His-Pro-Glu-His-Met-COOH GPDH Fig. 5. Sequence analysis of tiie carboxyl-terminal region of GPDH''-1 and СРОН^'-З. PTH-amino acids that were identified by high-performance liquid chromatography and/or by amino acid analysis after back-hydrolysis. The sequence of peptide Sp-1 was based on the qualitative identification of free amino acids after back-hydrolysis of all PTH-amino acids. —, the residue that was derived from amino acid composition analysis only. , the amino acid released quantitatively by carboxypeptidase A digestion of intact GPDH''-1 protein. The COOH- terminal sequence of rabbit muscle GPDH was from Otto et al [1977]. From Niesei et al [1982], with permission. the tryptic peptide maps, peptide T-1 was generated by residual chymotryptic activity, 3) Carboxypeptidase A digestion of GPDH^-1 released a leucyl residue quantitatively followed by the release of Asn/Gln, and 4) The se¬ quence of peptide T-1 from GPDH^-3 is identical to the carboxyl-terminal region of rabbit muscle GPDH [Otto et al, 1977] (Fig. 5). Therefore, the amino acid sequence of the first six residues of the carboxyl-terminal peptides T-1 are identical for GPDH'^-l and GPDH^-3, with peptide T-1 of GPDH^- 1 extended by the sequence Gln-Asn-Leu-COOH. The generation of each GPDH isozyme by a shortening at the carboxyl terminus could very likely account for the shift in physicochemical and kinetic Fig. 4. Tryptic peptide maps of oxidized GPDH^-1 and GPDH'^-3 isozymes. Peptides from 1.6 mg of GPDH''-! and 2.0 mg of GPDH^'-B protein were first developed chromatographically (pyridine/acetic acid/l-butanol/H20, 50:75:15:60, v/v/v/v) and then separated by electropho¬ resis at pH 4.4 (pyridine/acetic acid/acetone/H20, 1:2:8:40, v/v/v/v). Solid circles denote major peptide spots detected by fluorescamine staining and subsequently quantitated by amino acid analysis. Broken circles represent minor or unresolved peptides. Asterisk labeling represents deaminated peptides. The carboxyl-terminal peptides are indicated by hatching. From Niesel et al [1982], with permission.](https://iiif.wellcomecollection.org/image/b18019742_0066.JP2/full/800%2C/0/default.jpg)
