Purification and some properties of the fast migrating alkaline phosphatase in FL-amnion cells (the Kasahara isoenzyme) and its cDNA cloning
作者： Kazuya Higashino , Koji Muratani , Toshikazu Hada , Hiroyasu Imanishi , Yoshiki Amuro
DOI: 10.1016/0009-8981(90)90032-N
关键词: Untranslated region 、 Biology 、 Complementary DNA 、 Nucleic acid sequence 、 Restriction map 、 Clone (cell biology) 、 Alkaline phosphatase 、 Coding region 、 Biochemistry 、 Molecular biology 、 Northern blot
摘要: Abstract One of two main FL-amnion cell alkaline phosphatase (AP), the fast migrating one (FL-AP F ) has been reported to be identical Kasahara isoenzyme (K.I.), which occurs preferentially in sera patients with primary hepatoma. We purified FL-AP apparent molecular weight was 135 000 by gel filtration, and that subunit 62000 on SDS/PAGE, indicating homodimeric structure . found react monoclonal antibody against adult intestinal AP, but not placental AP. isolated cDNA clone from cells, 2525 base pairs length. Nucleotide sequence coding region 3' untranslated human AP cDNA. But 5' end slightly longer than Hence, (K.I.) may occur altered glycosylation
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