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. 1959 Jan;71(1):185–194. doi: 10.1042/bj0710185

Observations on the molecular weight and chemical composition of nisin A

G C Cheeseman 1, N J Berridge 1
PMCID: PMC1196767  PMID: 13628551

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Selected References

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

  1. BAVIN E. M., BEACH A. S., FALCONER R., FRIEDMANN R. Nisin in experimental tuberculosis. Lancet. 1952 Jan 19;1(6699):127–129. doi: 10.1016/s0140-6736(52)92429-x. [DOI] [PubMed] [Google Scholar]
  2. BERRIDGE N. J. Counter-current distribution of nisins. Nature. 1952 Apr 26;169(4304):707–708. doi: 10.1038/169707b0. [DOI] [PubMed] [Google Scholar]
  3. BERRIDGE N. J., NEWTON G. G. F., ABRAHAM E. P. Purification and nature of the antibiotic nisin. Biochem J. 1952 Dec;52(4):529–535. doi: 10.1042/bj0520529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BERRIDGE N. J. Preparation of the antibiotic nisin. Biochem J. 1949;45(4):486–493. doi: 10.1042/bj0450486. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. BLACKBURN S., LOWTHER A. G. The separation of N-2:4-dinitrophenly amino-acids on paper chromatograms. Biochem J. 1951 Jan;48(1):126–128. doi: 10.1042/bj0480126. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. CALLOW R. K., WORK T. S. Antibiotic peptides from Bacillus licheniformis; licheniformins A, B and C. Biochem J. 1952 Jul;51(4):558–568. doi: 10.1042/bj0510558. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. CHEESEMAN G. C., BERRIDGE N. J. An improved method of preparing nisin. Biochem J. 1957 Mar;65(3):603–608. doi: 10.1042/bj0650603. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. CRAIG L. C., GREGORY J. D., BARRY G. T. Studies on polypeptides and amino acids by countercurrent distribution. Cold Spring Harb Symp Quant Biol. 1950;14:24–31. doi: 10.1101/sqb.1950.014.01.005. [DOI] [PubMed] [Google Scholar]
  9. DU VIGNEAUD V., RESSLER C., TRIPPETT S. The sequence of amino acids in oxytocin, with a proposal for the structure of oxytocin. J Biol Chem. 1953 Dec;205(2):949–957. [PubMed] [Google Scholar]
  10. ELLIOTT D. F. A search for specific chemical methods for fission of peptide bonds. I. The N-acyl to O-acyl transformation in the degradation of silk fibroin. Biochem J. 1952 Feb;50(4):542–550. doi: 10.1042/bj0500542. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. HALSEY Y. D., NEURATH H. The terminal carboxyl groups of denatured yeast triosephosphate dehydrogenase. J Biol Chem. 1955 Nov;217(1):247–252. [PubMed] [Google Scholar]
  12. HIRSCH A. Various antibiotics from one strain of Streptococcus lactis. Nature. 1951 Jun 23;167(4260):1031–1032. doi: 10.1038/1671031a0. [DOI] [PubMed] [Google Scholar]
  13. LOWTHER A. G. Identification of N-2: 4-dinitrophenylamino-acids. Nature. 1951 May 12;167(4254):767–768. doi: 10.1038/167767b0. [DOI] [PubMed] [Google Scholar]
  14. MOORE S., STEIN W. H. A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. J Biol Chem. 1954 Dec;211(2):907–913. [PubMed] [Google Scholar]
  15. MOORE S., STEIN W. H. Chromatography of amino acids on sulfonated polystyrene resins. J Biol Chem. 1951 Oct;192(2):663–681. [PubMed] [Google Scholar]
  16. MOORE S., STEIN W. H. Procedures for the chromatographic determination of amino acids on four per cent cross-linked sulfonated polystyrene resins. J Biol Chem. 1954 Dec;211(2):893–906. [PubMed] [Google Scholar]
  17. NEWTON G. G. F., ABRAHAM E. P. Ayfivin and bacitracin: resolution of crude products into similar series of peptides. Biochem J. 1950 Sep;47(3):257–267. doi: 10.1042/bj0470257. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. NEWTON G. G. F., ABRAHAM E. P. Some properties of the bacitracin polypeptides. Biochem J. 1953 Mar;53(4):597–604. doi: 10.1042/bj0530597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. PARTRIDGE S. M., BRIMLEY R. C. Displacement chromatography on synthetic ion-exchange resins. VIII. A systematic method for the separation of amino-acids. Biochem J. 1952 Aug;51(5):628–639. doi: 10.1042/bj0510628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. SANGER F., THOMPSON E. O. P. The amino-acid sequence in the glycyl chain of insulin. II. The investigation of peptides from enzymic hydrolysates. Biochem J. 1953 Feb;53(3):366–374. doi: 10.1042/bj0530366. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. SANGER F. The terminal peptides of insulin. Biochem J. 1949;45(5):563–574. doi: 10.1042/bj0450563. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sanger F. The free amino groups of insulin. Biochem J. 1945;39(5):507–515. doi: 10.1042/bj0390507. [DOI] [PMC free article] [PubMed] [Google Scholar]

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