Full text
PDF


Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Blair T. T., Marini M. A., Agarwal S. P., Martin C. J. Succinylation of the amino group of isoleucine 16 in delta-chymotrypsin with retention of activity. FEBS Lett. 1971 Apr;14(2):86–88. doi: 10.1016/0014-5793(71)80106-0. [DOI] [PubMed] [Google Scholar]
- Borras F., Offord R. E. Protected intermediate for the preparation of semisynthetic insulins. Nature. 1970 Aug 15;227(5259):716–718. doi: 10.1038/227716a0. [DOI] [PubMed] [Google Scholar]
- Brandenburg D. Des-PheB1-Insulin, ein kristallines Analogon des Rinderinsulins. Hoppe Seylers Z Physiol Chem. 1969 Jun;350(6):741–750. doi: 10.1515/bchm2.1969.350.1.741. [DOI] [PubMed] [Google Scholar]
- Bünzli H. F., Bosshard H. R. Modification of the single arginine residue in insulin with phenylglyoxal. Hoppe Seylers Z Physiol Chem. 1971 Aug;352(8):1180–1182. [PubMed] [Google Scholar]
- DIXON H. B., MORET V. REMOVAL OF THE N-TERMINAL RESIDUE OF A PROTEIN AFTER TRANSAMINATION. Biochem J. 1965 Feb;94:463–469. doi: 10.1042/bj0940463. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dixon H. B. The preparation of N-(o-aminophenyl)aminomethanephosphonic acid. Biochem J. 1972 Nov;130(1):317–317. doi: 10.1042/bj1300317. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dixon H. B. Transamination of peptides. Biochem J. 1964 Sep;92(3):661–666. doi: 10.1042/bj0920661. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fields R., Dixon H. B. Micro method for determination of reactive carbonyl groups in proteins and peptides, using 2,4-dinitrophenylhydrazine. Biochem J. 1971 Feb;121(4):587–589. doi: 10.1042/bj1210587. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Marini M. A., Martin C. J. Chymotrypsin catalysis in the presence of formaldehyde. The pH-dependence of ester hydrolysis. Eur J Biochem. 1971 Mar 11;19(2):153–161. doi: 10.1111/j.1432-1033.1971.tb01299.x. [DOI] [PubMed] [Google Scholar]
- Maroux S., Desnuelle P. On some autolyzed derivatives of bovine trypsin. Biochim Biophys Acta. 1969 May;181(1):59–72. doi: 10.1016/0005-2795(69)90227-x. [DOI] [PubMed] [Google Scholar]
- SCHWERT G. W., TAKENAKA Y. A spectrophotometric determination of trypsin and chymotrypsin. Biochim Biophys Acta. 1955 Apr;16(4):570–575. doi: 10.1016/0006-3002(55)90280-8. [DOI] [PubMed] [Google Scholar]
- Stroud R. M., Kay L. M., Dickerson R. E. The crystal and molecular structure of DIP-inhibited bovine trypsin at2.7Angstrom resolution. Cold Spring Harb Symp Quant Biol. 1972;36:125–140. doi: 10.1101/sqb.1972.036.01.018. [DOI] [PubMed] [Google Scholar]
- WALSH K. A., NEURATH H. TRYPSINOGEN AND CHYMOTRYPSINOGEN AS HOMOLOGOUS PROTEINS. Proc Natl Acad Sci U S A. 1964 Oct;52:884–889. doi: 10.1073/pnas.52.4.884. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Woods K. R., Wang K. T. Separation of dansyl-amino acids by polyamide layer chromatography. Biochim Biophys Acta. 1967 Feb 21;133(2):369–370. doi: 10.1016/0005-2795(67)90078-5. [DOI] [PubMed] [Google Scholar]
- van Heyningen S., Tipton K. F., Dixon H. B. Transamination of the N-terminal residue of carboxypeptidase. Biochem J. 1968 Jul;108(3):508–509. doi: 10.1042/bj1080508. [DOI] [PMC free article] [PubMed] [Google Scholar]