Physicochemical properties of a beta-lactamase from Streptomyces UCSM-104.

A purified beta-lactamase from Streptomyces UCSM-104 shows the presence of three subforms when stained for protein and/or for activity after polyacrylamide gel electrophoresis or after electrofocusing. The pI values of the three subforms were 5.45, 5.30 and 5.10, respectively. The respective electrophoretic mobilities were 4.6 X 10(-5), 5.2 X 10(-5) and 5.9 X 10(-5)m2/sV. Relative molecular mass of 14,900 was determined. The amino acid composition was established. Cysteine was not detected. A fairly high proline content (8.3%) differentiates this enzyme from other beta-lactamases. Lysine was the only N-terminal amino acid detected after dansylation. The possible origin of the subforms is discussed.