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The effect of blocking amino groups on the susceptibility of BSA and calmodulin to high molecular weight protease (HMP) and calpain, the two major cytosolic proteases, was studied. Both proteases hydrolyzed methylated vs. unmodified BSA more slowly. Methylation of BSA resulted in the accumulation of proteolytic intermediates, especially of larger sizes. However, similar fragments were generated from unmodified BSA indicating that rates of hydrolysis rather that sites of proteolytic cleavage were altered. Calmodulin from Dictyostelium discoideum was hydrolyzed rapidly by HMP whereas brain and muscle calmodulins which have a epsilon-N-trimethyl residue on the single surface lysine were relatively stable.
K Murakami, and
J D Etlinger
January 1983,
Acta haematologica Polonica,
K Murakami, and
J D Etlinger
December 1991,
Agricultural and biological chemistry,
K Murakami, and
J D Etlinger
October 1981,
Scandinavian journal of immunology,
K Murakami, and
J D Etlinger
September 2005,
Molecular microbiology,
K Murakami, and
J D Etlinger
March 1991,
Biochemical and biophysical research communications,
K Murakami, and
J D Etlinger
October 1981,
Infection and immunity,
K Murakami, and
J D Etlinger
January 1961,
Acta physiologica Polonica,
K Murakami, and
J D Etlinger
January 2003,
Zeitschrift fur Naturforschung. C, Journal of biosciences,
K Murakami, and
J D Etlinger
August 1978,
Analytical biochemistry,
K Murakami, and
J D Etlinger
January 1974,
FEBS letters,
