TY - JOUR
T1 - Substrate specificity of a human-specific esterase
AU - Munjal, Devidayal
AU - Rose, Noel R.
N1 - Funding Information:
The authors’ are grateful to Dr. W. B. Elliott for donating some of the chromogenic substrates. by PHS Research Grant CA-05203 from The National tion No. 37 from The Center for Immunology.
PY - 1973/8
Y1 - 1973/8
N2 - A human species-specific esterase has been identified in tissues, cell cultures, and urine. It is the most slowly migrating (i.e., cathodal) of the esterase isoenzymes in agarose electrophoresis; it is not a choline estrase, a pseudocholine esterase, an acetyl phenylalanine-3-naphthyl esterase or N-benzoyl-arginine-3-naphthyl esterase. Hydrolysis of N-methyl indoxyl acetate caused by this esterase is not inhibited by eserine, eserine sulfate, or EDTA. Phenylmethylsulfonyl fluoride, however, did inhibit hydrolysis. Furthermore, this cathodal esterase does not show any chymotrypsin, trypsin, or leucine aminopeptidase enzyme activity.
AB - A human species-specific esterase has been identified in tissues, cell cultures, and urine. It is the most slowly migrating (i.e., cathodal) of the esterase isoenzymes in agarose electrophoresis; it is not a choline estrase, a pseudocholine esterase, an acetyl phenylalanine-3-naphthyl esterase or N-benzoyl-arginine-3-naphthyl esterase. Hydrolysis of N-methyl indoxyl acetate caused by this esterase is not inhibited by eserine, eserine sulfate, or EDTA. Phenylmethylsulfonyl fluoride, however, did inhibit hydrolysis. Furthermore, this cathodal esterase does not show any chymotrypsin, trypsin, or leucine aminopeptidase enzyme activity.
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U2 - 10.1016/0003-2697(73)90380-1
DO - 10.1016/0003-2697(73)90380-1
M3 - Article
C2 - 4198962
AN - SCOPUS:0015791904
SN - 0003-2697
VL - 54
SP - 502
EP - 506
JO - Analytical biochemistry
JF - Analytical biochemistry
IS - 2
ER -