Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure.
Tartrate-resistant acid phosphatase type-5 was purified to apparent homogeneity from human osteoclastomas by sequential chromatography on CM-Sepharose, Phenyl-Sepharose, concanavalin A-Sepharose, FPLC Superose-12, and FPLC Mono-S. The purification over the original tissue extract was 1167-fold, with a yield of 16%. An identity in the N-terminal amino acid sequence and Mr was found between this enzyme and two type-5 tartrate-resistant acid phosphatases isolated from hairy cell leukemia spleen. However, they appeared to be different as assessed by amino acid composition. In contrast to a previous report, no evidence was found for two subunits of the tartrate-resistant acid phosphatase.
Stepan
J J
JJ
Department of Medicine, Loma Linda University, CA.
Lau
K H
KH
Mohan
S
S
Singer
F R
FR
Baylink
D J
DJ
D000135:Acid Phosphatase / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D002845:Chromatography; D004351:Drug Resistance; D005870:Giant Cell Tumors / Q000201:enzymology*; D006801:Humans; D007943:Leukemia, Hairy Cell / Q000201:enzymology*; D008969:Molecular Sequence Data; D013644:Tartrates / Q000302:isolation & purification*
D013644:Tartrates; D000135:Acid Phosphatase