The Lysozyme of Bacteriophage λ
1969; Elsevier BV; Volume: 244; Issue: 8 Linguagem: Inglês
10.1016/s0021-9258(18)94355-3
ISSN1083-351X
AutoresLindsay W. Black, David S. Hogness,
Tópico(s)Enzyme Structure and Function
ResumoAbstract The frequencies of the amino acid residues in λ-lysozyme have been determined. A molecular weight of 17.9 x 103 was computed from these frequencies, in agreement with the value determined previously from the sedimentation behavior of this enzyme. Analyses of the amino-terminal residues by the cyanate method and of the carboxyl-terminal residues by hydrazinolysis and by exposure to carboxypeptidase A indicate that λ-lysozyme consists of a single polypeptide chain containing 159 residues bounded by methionine at the amino terminus and valine at the carboxyl terminus. It contains no disulfide bonds. The λ-lysozyme exhibits similarities with the lysozymes of coliphages T2 and T4 in regard to total number of residues, their distribution among different groups of amino acids, the lack of disulfide bonds, and the nature of the amino terminus. In addition, a weak immunochemical cross-reaction between the λ- and T4-lysozymes was shown.
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