Search

A direct reading, six channel conductivity recording apparatus has been constructed and used to assay enzymes, including some of those found in muscle. This paper gives the essential theory of the method, and indicates that it is a highly versatile assay system. It may be applicable whenever ionic substrates are involved, but this is more easily tested by experiment than by calculation. The manipulation involved in an assay is probably less than in any other method. Conductimetry could be used as a kinetic method for some enzymes (for example amidases), but suffers from restrictions in the amounts of non-reacting ionic species which can be tolerated. Improvements in the temperature control of the apparatus could allow much higher sensitivity to be used. [ABSTRACT FROM AUTHOR]

Immunological resemblance between the endopeptidase, endo-β-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase of lysostaphin has been demonstrated. Only the peptidase was found to give precipitin reaction. All three enzymes sensitized tanned sheep erythrocytes to agglutination in homologous and heterologous enzyme antisera. Absorption experiments revealed the presence of specific determinant(s) in all the enzymes, determinant(s) shared between two and two enzymes, and a possible deterrninant(s)-common to all three enzymes. [ABSTRACT FROM AUTHOR]

The analysis of a monoclinic crystal modification of L-asparaginase from Eseherichia coli supports the chemical and physico-chemical evidence for a tetrameric subunit structure. The pseudo-symmetries occurring in the crystal structure provide evidence that the molecules lie on positions with approximate point symmetry 222. [ABSTRACT FROM AUTHOR]