Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1974 Apr;139(1):1–10. doi: 10.1042/bj1390001

The tryptic peptides of rabbit muscle triose phosphate isomerase

P H Corran 1, S G Waley 1
PMCID: PMC1166244  PMID: 4618774

Abstract

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.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bloemendal H., Berns A. J., van der Ouderaa F., de Jong W. W. Evidence for a "non-genetic" origin of the A1 chains of alpha-crystallin. Exp Eye Res. 1972 Jul;14(1):80–81. doi: 10.1016/0014-4835(72)90147-9. [DOI] [PubMed] [Google Scholar]
  2. Burton P. M., Waley S. G. Studies on the sub-units of triose phosphate isomerase. Biochem J. 1968 May;107(6):737–744. doi: 10.1042/bj1070737. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Corran P. H., Waley S. G. The amino acid sequence of rabbit muscle triose phosphate isomerase. FEBS Lett. 1973 Feb 15;30(1):97–99. doi: 10.1016/0014-5793(73)80627-1. [DOI] [PubMed] [Google Scholar]
  4. Delcour J., Papaconstantinou J. Biochemistry of bovine lens proteins. IV. Synthesis and aggregation of -crystallin subunits in differentiating lens cells. J Biol Chem. 1972 May 25;247(10):3289–3295. [PubMed] [Google Scholar]
  5. Furth A. J., Milman J. D., Priddle J. D., Offord R. E. Studies on the subunit structure and amino acid sequence of trisoe phosphate isomerase from chicken breast muscle. Biochem J. 1974 Apr;139(1):11–22. doi: 10.1042/bj1390011. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gray W. R., Smith J. F. Rapid sequence analysis of small peptides. Anal Biochem. 1970 Jan;33(1):36–42. doi: 10.1016/0003-2697(70)90436-7. [DOI] [PubMed] [Google Scholar]
  7. Hartley B. S. Strategy and tactics in protein chemistry. Biochem J. 1970 Oct;119(5):805–822. doi: 10.1042/bj1190805f. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hartman F. C. Haloacetol phosphates. Characterization of the active site of rabbit muscle triose phosphate isomerase. Biochemistry. 1971 Jan 5;10(1):146–154. doi: 10.1021/bi00777a021. [DOI] [PubMed] [Google Scholar]
  9. Jörnvall H. Horse liver alcohol dehydrogenase. The primary structure of an N-terminal part of the protein chain of the ethanol-active isoenzyme. Eur J Biochem. 1970 Jul;14(3):521–534. doi: 10.1111/j.1432-1033.1970.tb00319.x. [DOI] [PubMed] [Google Scholar]
  10. Krietsch W. K., Pentchev P. G., Klingenburg H. The isolation and characterization of the isoenzymes of rabbit-muscle triosephosphate isomerase. Eur J Biochem. 1971 Nov 11;23(1):77–85. doi: 10.1111/j.1432-1033.1971.tb01594.x. [DOI] [PubMed] [Google Scholar]
  11. Krietsch W. K., Pentchev P. G., Klingenbürg H., Hofstätter T., Bücher T. The isolation and crystallization of yeast and rabbit liver triose phosphate isomerase and a comparative characterization with the rabbit muscle enzyme. Eur J Biochem. 1970 Jun;14(2):289–300. doi: 10.1111/j.1432-1033.1970.tb00289.x. [DOI] [PubMed] [Google Scholar]
  12. Lai C. Y., Chen C., Horecker B. L. Primary structure of two COOH-terminal hexapeptides from rabbit muscle aldolase: a difference in the structure of the alpha and beta subunits. Biochem Biophys Res Commun. 1970 Jul 27;40(2):461–468. doi: 10.1016/0006-291x(70)91031-4. [DOI] [PubMed] [Google Scholar]
  13. Lee E. W., Barriso J. A., Pepe M., Snyder R. Purification and properties of liver triose phosphate isomerase. Biochim Biophys Acta. 1971 Jul 21;242(1):261–267. doi: 10.1016/0005-2744(71)90106-9. [DOI] [PubMed] [Google Scholar]
  14. McDonald J. K., Zeitman B. B., Reilly T. J., Ellis S. New observations on the substrate specificity of cathepsin C (dipeptidyl aminopeptidase I). Including the degradation of beta-corticotropin and other peptide hormones. J Biol Chem. 1969 May 25;244(10):2693–2709. [PubMed] [Google Scholar]
  15. Midelfort C. F., Mehler A. H. Deamidation in vivo of an asparagine residue of rabbit muscle aldolase. Proc Natl Acad Sci U S A. 1972 Jul;69(7):1816–1819. doi: 10.1073/pnas.69.7.1816. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Miller J. C., Waley S. G. Amino acid sequences around the cysteine residues of rabbit muscle triose phosphate isomerase. Biochem J. 1971 Apr;122(2):209–218. doi: 10.1042/bj1220209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Miller J. C., Waley S. G. The active centre of rabbit muscle triose phosphate isomerase. The site that is labelled by glycidol phosphate. Biochem J. 1971 Jun;123(2):163–170. doi: 10.1042/bj1230163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Norton I. L., Pfuderer P., Stringer C. D., Hartman F. C. Isolation and characterization of rabbit muscle triose phosphate isomerase. Biochemistry. 1970 Dec 8;9(25):4952–4958. doi: 10.1021/bi00827a019. [DOI] [PubMed] [Google Scholar]
  19. Offord R. E. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups. Nature. 1966 Aug 6;211(5049):591–593. doi: 10.1038/211591a0. [DOI] [PubMed] [Google Scholar]
  20. Rowlands R. J., Lindley H. A theoretical investigation into the potential usefulness of the cathepsin C 'domino' technique. Biochem J. 1972 Feb;126(3):685–688. doi: 10.1042/bj1260685. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Rozacky E. E., Sawyer T. H., Barton R. A., Gracy R. W. Studies on human triosephosphate isomerase. I. Isolation and properties of the enzyme from erythrocytes. Arch Biochem Biophys. 1971 Sep;146(1):312–320. doi: 10.1016/s0003-9861(71)80069-3. [DOI] [PubMed] [Google Scholar]
  22. Shotton D. M., Hartley B. S. Amino-acid sequence of porcine pancreatic elastase and its homologies with other serine proteinases. Nature. 1970 Feb 28;225(5235):802–806. doi: 10.1038/225802a0. [DOI] [PubMed] [Google Scholar]
  23. WALEY S. G., WATSON J. The action of trypsin on polylysine. Biochem J. 1953 Sep;55(2):328–337. doi: 10.1042/bj0550328. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES