Phenylmethylsulfonyl fluoride stimulates proteolysis of nuclear proteins from chick liver.
The degradation of H1 histone and high mobility group (HMG) nonhistone proteins was stimulated when the homogenate from chick liver was incubated in the presence of phenylmethylsulfonyl fluoride (PMSF). Two proteinase inhibitors, elastatinal and chymostatin, significantly inhibited the PMSF-stimulated degradation of H1 histone and HMG proteins. On the contrary, other proteinase inhibitors like leupeptin, pepstatin, trypsin inhibitor, antipain, o-phenanthroline and EDTA had no effect on the degradation of the nuclear proteins. These results warn the researcher to be cautious while using PMSF for preparation of nuclear proteins such as H1 histone and HMG proteins.
Oka
T
T
Department of Nutrition, School of Medicine, University of Tokushima, Japan.
Thakur
M K
MK
Miyamoto
K
K
Sassa
T
T
Suzuki
I
I
Natori
Y
Y
D000818:Animals; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D006609:High Mobility Group Proteins / Q000302:isolation & purification / Q000378:metabolism*; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism*; D015151:Immunoblotting; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology*; D011480:Protease Inhibitors / Q000494:pharmacology*
D006609:High Mobility Group Proteins; D006657:Histones; D011480:Protease Inhibitors; D010664:Phenylmethylsulfonyl Fluoride