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C. Anfinsen, M. Sela, H. Tritch (1956)
A method for the specific proteolytic cleavage of protein chains.Archives of biochemistry and biophysics, 65 1
V. Zahn, Otto Waschka (1956)
Reaktionen von bisdiazohexan mit aminosäuren, mercaptanen, wollkeratin und seidenfibroinMacromolecular Chemistry and Physics, 18
(1957)
Laby, Tables of Phvsical and Chemical Constants
J. Jollés-Thaureaux, P. Jollès, C. Fromageot (1958)
Structure du lysozyme d'oeuf de poule. Etude des peptides de l'hydrolysat trypsique☆Biochimica et Biophysica Acta, 27
R. Canfield (1963)
THE AMINO ACID SEQUENCE OF EGG WHITE LYSOZYME.The Journal of biological chemistry, 238
V. Zahn, J. Meienhofer (1958)
Reaktionen von 1,5-difluor-2,4-dinitrobenzol mit insulin 1. Mitt. Synthese von modellverbindungenMacromolecular Chemistry and Physics, 26
M. Sela, F. White, C. Anfinsen (1959)
The reductive cleavage of disulfide bonds and its application to problems of protein structure.Biochimica et biophysica acta, 31 2
H. Zahn, H. Zuber, Waldemar Ditscher, Dieter Wegerle, J. Meienhofer (1956)
Reaktion von p,p′-Difluor-m,m′-dinitro-diphenylsulfon mit SeidenfibroinChemische Berichte, 89
S. Gurin, H. Clarke (1934)
ALLOCATION OF THE FREE AMINO GROUPS IN PROTEINS AND PEPTIDESJournal of Biological Chemistry, 107
David Smith, G. Wood, P. Charlwood (1956)
APPLICATION OF THE ARCHIBALD ULTRACENTRIFUGAL PROCEDURE TO LYSOZYME AND APURINIC ACID: EVALUATION USING A MECHANICAL INTEGRATORCanadian Journal of Chemistry, 34
K. Poduska, J. Rudinger, F. Šorm (1955)
Amino-acids and peptides. XVI. Peptides of DL-α,β-diaminopropionic acidCollection of Czechoslovak Chemical Communications, 20
(1934)
Collection Czech
It was established that phenol‐2,4‐disulfonyl chloride and α‐naphthol‐2, 4‐disulfonyl chloride introduce new intramolecular or tertiary bonds into lysozyme. The phenolic hydroxyl group seems to make the cross linking reagents soluble in aqueous media; it was established that a sulfonylating; species does dissolve prior to hydrolysis but that the chlorosulfonyl groups are hydrolyzed within seconds of dissolution. New covalently linked residues were shown to be introduced by different, spectra. Peptide maps of the lysozyme treated with phenol‐2,4‐disulfonyl chloride. peroxidized, and digested with trypsin showed definite deletions and additions when compared with the control. Partial analysis of the peptides showed that cross linking between ε‐amino groups of lysine residues had occurred. A certain degree of stabilization of lysozyme to inactivation by certain inactivating conditions was noted after treatment with the two reagents. Ultra‐centrifugal analysis of the lysozyme treated with phenol‐2,4‐disulfonyl chloride showed that there was no detectable fraction having a higher molecular weight than native lysozyme. Tentative assignments of positions of cross linking were made.
Biopolymers – Wiley
Published: Aug 1, 1964
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