PubMed · 4288607
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
W James, B Moule. 1966. Hypophosphatasia.. https://doi.org/10.1016/s0009-9260(66)80056-9
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Marine picocyanobacteria of the genera Prochlorococcus and Synechococcus, the two most abundant phototrophs on Earth, thrive in oligotrophic oceanic regions. While it is well known that specific lineages are exquisitely adapted to prevailing in situ light and temperature regimes, much less is known of the molecular machinery required to facilitate occupancy of these low-nutrient environments. Here, we describe a hitherto unknown alkaline phosphatase, Psip1, that has a substantially higher affinity for phosphomonoesters than other well-known phosphatases like PhoA, PhoX, or PhoD and is restricted to clade III Synechococcus and a subset of high light I-adapted Prochlorococcus strains, suggesting niche specificity. We demonstrate that Psip1 has undergone convergent evolution with PhoX, requiring both iron and calcium for activity and likely possessing identical key residues around the active site, despite generally very low sequence homology. Interrogation of metagenomes and transcriptomes from TARA oceans and an Atlantic Meridional transect shows that psip1 is abundant and highly expressed in picocyanobacterial populations from the Mediterranean Sea and north Atlantic gyre, regions well recognized to be phosphorus (P)-deplete. Together, this identifies psip1 as an important oligotrophy-specific gene for P recycling in these organisms. Furthermore, psip1 is not restricted to picocyanobacteria and is abundant and highly transcribed in some α-proteobacteria and eukaryotic algae, suggesting that such a high-affinity phosphatase is important across the microbial taxonomic world to occupy low-P environments.
PURPOSE: To evaluate the ability of monoclonal antibodies against alkaline phosphatase (AL-P) for tumor immunolocalization in nude mice. MATERIALS AND METHODS: Two monoclonal antibodies against placental alkaline phosphatase (PLAP) and liver alkaline phosphatase (LAP) were intravenously administered to nude mice bearing AL-P producing HeLa Hep 2 tumors. Sera and tumors from 65 patients with testicular germ cell tumors were examined for PLAP levels. RESULTS: Levels of PLAP or LAP in the HeLa xenografts were shown to be comparable to levels of PLAP in seminomas, including lymph node metastases, or nonseminomas, respectively. A biodistribution study showed that the percentage of the injected dose of I-125 labelled anti-PLAP in the xenografts was rather constant at around 7% until 7 days after injection, while the percentage of the injected dose of I-125 labelled anti-LAP MAb decreased with time as in other tissues which do not contain significant amounts of PLAP or LAP. On scintiscan, the xenografts in nude mice were distinctly visualized at 7 days after injection of anti-PLAP MAb. CONCLUSIONS: These data may support the potential use of the anti-PLAP MAb for the immunodetection of lymph node metastases of seminoma.
Structurally intact and functionally active human bone alkaline phosphatase was isolated from clavicle fragments of IDU, an Egyptian mummy of the Old Kingdom (2150 +/- 50 BC). Both anion exchange and affinity chromatographies were employed to optimise the preparation of the ancient enzyme resulting in a specific activity of 180 +/- 30 mU/mg. The intactness of the bone enzyme fractions of the wheat-germ lectin affinity chromatography was successfully demonstrated in an ELISA using the monoclonal antibody BAP A. Fortunately, the mummified bone was not contaminated by fungi or bacteria.