Structural comparisons of two allelic variants of human placental alkaline phosphatase
✍ Scribed by JoséLuis Millán; Torgny Stigbrand; Hans Jörnvall
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 695 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0020-711X
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Human placental alkaline phosphatase is a membrane-anchored dimeric protein. Unfolding of the enzyme by guanidinium chloride (GdmCl) caused a decrease of the fluorescence intensity and a large red-shifting of the protein fluorescence maximum wavelength from 332 to 346 nm. The fluorescence changes we
## Abstract A monoclonal antibody (H317) with specificity for the heat‐stable placental‐type alkaline phosphatase (Pl‐ALP) isoenzyme has been used to investigate the occurrence of Pl‐ALP in patients with primary breast carcinoma. All pre‐operative plasma samples were negtive for Pl‐ALP in a sensiti