A novel combination of two classic catalytic schemes.

A genetic disorder of rabbits consisting of a deficiency of the enzyme lysozyme is characterized. The condition appears to be inherited as an autosomal recessive trait. Most of the tissues of lysozyme-deficient rabbits including bone marrow, liver, lung. spleen and bone had levels of lysozyme which were 1% or less of the levels in the corresponding tissues of normal rabbits when measured with the lysoplate method. Levels of lysozyme in the kidney and serum were 6% of controls, but the thymus of the lysozyme-deficient rabbits had normal levels of the enzyme. All leukocytes of the lysozyme-deficient rabbits were negative for lysozyme when examined by a histobacterial technic. No morphologic lesions could be detected in any of the tissues of the lysozyme-deficient rabbits. Although several species of animals have been reported to be lysozyme deficient, this appears to be the first report of lysozyme deficiency occurring as a mutant condition. It is suggested that these mutant rabbits may be useful as a resource for experiments designed to delineate the biologic role of lysozyme.

Lysozyme deficiency-an inherited disorder of rabbits.

The role of carboxyl groups on the chitosanase and CMCase activity of a bifunctional enzyme purified from a commercial cellulase with EDC modification

Modified target molecules are disclosed comprising genetically modified molecules, preferably enzymes, that include a catalytic triad which alters the performance of the polypeptide. Optionally, such a catalytic triad in the modified target molecule comprises three members equivalent to amino acid residues Serine 227, Histidine 200, or Glutamate 139, respectively, in the Bacillus cellulase 103 sequence. Using the embodiments disclosed by the present invention, altered performance profiles, such as enzyme activity or stability, under alkaline conditions can be achieved. Methods of making and using modified target molecules are also disclosed.

Modified target enzymes having catalytic triads and uses thereof

On the stereochemical basis of enzyme action: lessons from lysozyme.

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On the stereochemical basis of enzyme action: lessons from lysozyme.