Preparations and immunological characterizations of two lysozyme derivatives dinitrophenylated at lysine-33 and lysine-96, respectively.

Preparations and immunological characterizations of two lysozyme derivatives dinitrophenylated at lysine-33 and lysine-96, respectively. Research Abstract Details 

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Preparations and immunological characterizations of two lysozyme derivatives dinitrophenylated at lysine-33 and lysine-96, respectively. Abstract Text:

A Hirayama,H Fujio,Y Dohi,Y Takagaki,K Kondo,T Amano,

Two derivatives of hen egg-white lysozyme (lysozyme) with single substitutions of a 2,4-dinitrophenyl (DNP) residue were prepared. The reaction of lysozyme with a 10-fold molar excess of 2,4-dinitrobenzene sulfonic acid provided one mono-DNP substituted lysozyme (DNP1-33lysozyme), which was purified by ion-exchange chromatographies. The other one (DNP1-96lysozyme) was prepared as follows. After maleylation of lysozyme in the presence of a 7-fold molar excess of maleic anhydride, the derivative with one free amino group was purified on DE-52. This material was dinitrophenylated with 2,4-dinitrobenzene sulfonic acid and the mono-DNP substituted derivative was purified on DE-52. DNP1-96lysozyme was finally purified on SE-Sephadex C-25, after demaleylation at pH 3.5, at 37 degrees C, for 5 days. DNP1-33lysozyme and DNP1-96lysozyme each migrated as a single band with slower mobility than that of native lysozyme. On reduction, carboxymethylation and chymotrypsin digestion, both mono-DNP substituted lysozymes yielded a single yellow peptide. The amino acid compositions or partial sequence of these peptides indicated that lysine-33 and lysine-96 were the only dinitrophenylated residues in DNP1-33lysozyme and DNP1-96lysozyme, respectively. DNP1-33lysozyme and DNP1-96lysozyme showed antigenic reactivities equal to that of native lysozyme with antisera to lysozyme. The DNP residues on the protein were accessible to anti-DNP antibodies, but the affinities of DNP1-33lysozyme to anti-DNP antibodies were lower than those of DNP1-96lysozyme. This result is discussed with respect to the local environments of the DNP residues in these proteins.

Preparations and immunological characterizations of two lysozyme derivatives dinitrophenylated at lysine-33 and lysine-96, respectively. Publishing Authors By Initials

A Hirayama,H Fujio,Y Dohi,Y Takagaki,K Kondo,T Amano,

For similar enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: muramidase research abstracts see: enzymes and coenzymes: enzymes: hydrolases: glycoside hydrolases: muramidase research

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Preparations and immunological characterizations of two lysozyme derivatives dinitrophenylated at lysine-33 and lysine-96, respectively. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 89

Page Numbers: 963-74

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Mar

YEAR: 1981

Preparations and immunological characterizations of two lysozyme derivatives dinitrophenylated at lysine-33 and lysine-96, respectively. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Preparations and immunological characterizations of two lysozyme derivatives dinitrophenylated at lysine-33 and lysine-96, respectively. Keywords Mesh Terms:

KEYWORDS: Muramidase

MESH TERMS: immunology

Chemical & Substance for Abstract: Preparations and immunological characterizations of two lysozyme derivatives dinitrophenylated at lysine-33 and lysine-96, respectively. Information

Substance Name: Muramidase

Registry Number: EC 3.2.1.17

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Country: JAPAN

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MEDLINETA: J Biochem

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