He. Stubberud et al., Purification and partial characterisation of tentatively classified acid phosphatase from the earthworm Eisenia veneta, COMP BIOC B, 126(4), 2000, pp. 487-494
Citations number
39
Categorie Soggetti
Biochemistry & Biophysics
Journal title
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
In order to use leakage of lysosomal acid phosphatase (AP) as a biomarker o
f stress to earthworms. more information about AP's in earthworms are neede
d. This paper describes the details about tentatively classified APs in the
earthworm Eisenia veneta. Two isoenzymes (enzyme I and II) of acid phospha
tase (AP) and one alkaline phosphatase (enzyme III) from the earthworm E. v
eneta were separated by gel filtration. All three enzymes were further puri
fied and concentrated on a Con A Sepharose 4B column. Enzyme I was inhibite
d by tartrate, showed an optimal pH range between 4.0 and 5.0 and was assum
ed to be of lysosomal origin. Enzyme II was the major enzyme showing the hi
ghest activity of the three enzymes. It was expected to be a lysosomal AP u
nder physiological conditions. Enzyme II had a molecular mass 113 kDa and w
as composed of apparently identical polypeptide chains of 36 kDa each. This
enzyme was inhibited by tartrate, showed an optimal pH in the range 6.0-7.
5 and was slowly degraded at temperatures above 40 degrees C. Enzyme III is
not inhibited by tartrate and has a pH-optimum > 9. The subcellular locati
on under physiological conditions was assumed to be the cytosol. (C) 2000 E
lsevier Science Inc. All rights reserved.