Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1954 Oct;58(2):227–231. doi: 10.1042/bj0580227

The liberation of aspartic acid during the acid hydrolysis of proteins

S Blackburn 1, G R Lee 1
PMCID: PMC1269876  PMID: 13208577

Full text

PDF
227

Selected References

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

  1. ACHER R., FROMAGEOT C., JUTISZ M. Séparations chromatographiques d'acides aminés et de peptides; les acides aminés et de peptides; les acides aminés individuels de l'insuline avec une note sur le dosage de la proline. Biochim Biophys Acta. 1950 Mar;5(1):81–88. doi: 10.1016/0006-3002(50)90151-x. [DOI] [PubMed] [Google Scholar]
  2. ACHER R., JUTISZ M., FROMAGEOT C. Sur la structure du lysozyme; étude de la libération des groupes fonctionnels et des acides aminés au cours d'une hydrolyse acide ménagée. Biochim Biophys Acta. 1950 Jun;5(3/4):493–498. doi: 10.1016/0006-3002(50)90195-8. [DOI] [PubMed] [Google Scholar]
  3. BLACKBURN S., LOWTHER A. G. The action of organic acids on some fibrous proteins: the oxidation of wool keratin. Biochem J. 1951 Sep;49(4):554–559. doi: 10.1042/bj0490554. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BLACKBURN S., ROBSON A. A radio-chemical method for the micro-estimation of alpha-amino-acids separated on paper partition chromatograms. Biochem J. 1953 May;54(2):295–299. doi: 10.1042/bj0540295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. BLACKBURN S. The action of papain on wool keratin. Biochem J. 1950 Oct;47(4):443–451. doi: 10.1042/bj0470443. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. BLACKBURN S. The use of buffered columns in the chromatographic separation of 2:4-dinitrophenyl amino acids. Biochem J. 1949;45(5):579–584. doi: 10.1042/bj0450579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Blackburn S., Consden R., Phillips H. The action of sulphites on the cystine disulphide linkages of wool: 4. Methylation of the thiol groups of bisulphited wools. Biochem J. 1944;38(1):25–29. doi: 10.1042/bj0380025. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Consden R., Gordon A. H., Martin A. J. A study of the acidic peptides formed on the partial acid hydrolysis of wool. Biochem J. 1949;44(5):548–560. doi: 10.1042/bj0440548. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Consden R., Gordon A. H., Martin A. J. Gramicidin S: the sequence of the amino-acid residues. Biochem J. 1947;41(4):596–602. [PMC free article] [PubMed] [Google Scholar]
  10. DESNUELLE P., BONJOUR G. Quelques modèles simples pour l'étude de l'hydrolyse protéique en milieu faiblement acide. Biochim Biophys Acta. 1952 Oct;9(4):356–361. doi: 10.1016/0006-3002(52)90179-0. [DOI] [PubMed] [Google Scholar]
  11. Dent C. E. A study of the behaviour of some sixty amino-acids and other ninhydrin-reacting substances on phenol-;collidine' filter-paper chromatograms, with notes as to the occurrence of some of them in biological fluids. Biochem J. 1948;43(2):169–180. [PMC free article] [PubMed] [Google Scholar]
  12. Gordon A. H., Martin A. J., Synge R. L. A study of the partial acid hydrolysis of some proteins, with special reference to the mode of linkage of the basic amino-acids. Biochem J. 1941 Dec;35(12):1369–1387. doi: 10.1042/bj0351369. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. PARTRIDGE S. M., DAVIS H. F. Preferential release of aspartic acid during the hydrolysis of proteins. Nature. 1950 Jan 14;165(4185):62–62. doi: 10.1038/165062a0. [DOI] [PubMed] [Google Scholar]
  14. Polson A., Mosley V. M., Wyckoff R. W. The Quantitative Chromatography of Silk Hydrolysate. Science. 1947 Jun 6;105(2736):603–604. doi: 10.1126/science.105.2736.603. [DOI] [PubMed] [Google Scholar]
  15. SANGER F., TUPPY H. The amino-acid sequence in the phenylalanyl chain of insulin. I. The identification of lower peptides from partial hydrolysates. Biochem J. 1951 Sep;49(4):463–481. doi: 10.1042/bj0490463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. THOMPSON A. The c-terminal residue of lysozyme. Nature. 1952 Mar 22;169(4299):495–496. doi: 10.1038/169495a0. [DOI] [PubMed] [Google Scholar]
  17. THOMPSON E. O. The N-terminal sequence of carboxypeptidase. Biochim Biophys Acta. 1953 Apr;10(4):633–634. doi: 10.1016/0006-3002(53)90314-x. [DOI] [PubMed] [Google Scholar]
  18. WAELSCH H. Certain aspects of intermediary metabolism of glutamine, asparagine, and glutathione. Adv Enzymol Relat Subj Biochem. 1952;13:237–319. doi: 10.1002/9780470122587.ch7. [DOI] [PubMed] [Google Scholar]

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

RESOURCES