The N-terminal groups of calf-thymus histones
- 1 January 1958
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 68 (1) , 35-40
- https://doi.org/10.1042/bj0680035
Abstract
The chief N-terminal groups of the histones extracted from calf-thymus glands are proline and alanine, with smaller amounts of lysine and serine, and still less of 6 other amino acids. The proportions of the serine and lysine end groups have declined markedly in later preparations of the histones. The quantities of the end groups gave an average weight of about 25000/gram molecule of end groups. In a fractionation of the histones, those precipitated by NaCl-NH3 (the arginine-rich histones) mostly have alanine N-terminal groups, whereas those remaining in solution in NaCl-NHg (the lysine-rich histones) mostly have proline end groups.Keywords
This publication has 15 references indexed in Scilit:
- Products of hydrolysis of dinitrophenylproline and N-terminal proline-peptides with hydrochloric acidBiochemical Journal, 1956
- CHROMATOGRAPHIC FRACTIONATION OF CALF THYMUS HISTONEJournal of Biological Chemistry, 1955
- HISTONES WITH HIGH LYSINE CONTENTThe Journal of general physiology, 1955
- CORTICOTROPINS (ACTH) .2. AMINO ACID COMPOSITION OF ALPHA-CORTICOTROPIN1955
- The fractionation and composition of histones from thymus nucleoproteinBiochimica et Biophysica Acta, 1954
- The histones of calf thymus deoxyribonucleoprotein II. Electrophoretic and semimentation behaviour and a partial fractionationBiochimica et Biophysica Acta, 1954
- A Paper Chromatographic Method for the Quantitative Estimation of Amino-AcidsNature, 1954
- The N-terminal sequence of carboxypeptidaseBiochimica et Biophysica Acta, 1953
- The separation of N-2:4-dinitrophenyl amino-acids on paper chromatogramsBiochemical Journal, 1951
- The free amino groups of haemoglobinsBiochemical Journal, 1948