A 100-kDa antigen recognized by a newly prepared monoclonal antibody specific to the vanadocytes of the vanadium-rich ascidian, Ascidia sydneiensis samea, is glycogen phosphorylase
T. Uyama et al., A 100-kDa antigen recognized by a newly prepared monoclonal antibody specific to the vanadocytes of the vanadium-rich ascidian, Ascidia sydneiensis samea, is glycogen phosphorylase, ZOOL SCI, 15(6), 1998, pp. 815-821
Ascidians have the unusual physiological ability to accumulate high levels
of vanadium and reduce it to the +3 oxidation state (V-III) in vanadocytes,
the vanadium-containing blood cells. We are characterizing several polypep
tides specific to vanadocytes that may participate in this. This study reve
aled that a 100-kDa antigen, recognized by a newly prepared monoclonal anti
body, S8E4, is exclusively localized in vanadocytes, and identified the ant
igen as glycogen phosphorylase (EC 2.4.1.1) by sequencing the encoded cDNA.
Since two enzymes, glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and 6-p
hosphogluconate dehydrogenase (EC 1.1.1.44), both in the pentose phosphate
pathway, have already been identified in vanadocytes, at least three enzyme
s involved in carbohydrate metabolism are localized in vanadocytes in huge
amounts.