Shrimp Alkaline Phosphatase (SAP)
Descriptive papers
de Backer M.M., McSweeney S., Lindley P.F., Hough E. (2004): Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase. Acta Crystallogr D Biol Crystallogr. Sep;60(Pt 9):1555-61. Epub 2004 Aug 26.
Nilsen I.W., Øverbø K., Olsen R.L. (2001): Thermolabile alkaline phosphatase from Northern shrimp (Pandalus borealis): protein and cDNA sequence analyses. Comp Biochem Physiol B Biochem Mol Biol. Jul;129(4):853-61.
Papers showing use of SAP
Degradering of nucleotides before genotyping or sequencing
Millis M.P. (2011): Medium-throughput SNP genotyping using mass spectrometry: multiplex SNP genotyping using the iPLEX® Gold assay. Methods Mol Biol. 700:61-76.
Schaeffeler E., Zanger U.M., Eichelbaum M., Asante-Poku S., Shin J.G., Schwab M. (2008): Highly multiplexed genotyping of thiopurine s-methyltransferase variants using MALD-TOF mass spectrometry: reliable genotyping in different ethnic groups. Clin Chem. Oct;54(10):1637-47. Epub 2008 Aug 7.
Ahlford A., Kjeldsen B., Reimers J., Lundmark A., Romani M., Wolff A., Syvänen A.C., Brivio M. (2010): Dried reagents for multiplex genotyping by tag-array minisequencing to be used in microfluidic devices. Analyst. Sep;135(9):2377-85. Epub 2010 Jul 29.
Vallone P.M., Fahr K., Kostrzewa M. (2005): Genotyping SNPs using a UV-photocleavable oligonucleotide in MALDI-TOF MS. Methods Mol Biol. 297:169-78.
Zhou G.H., Shirakura H., Kamahori M., Okano K., Nagai K., Kambara H. (2004): A gel-free SNP genotyping method: bioluminometric assay coupled with modified primer extension reactions (BAMPER) directly from double-stranded PCR products. Hum Mutat. ug;24(2):155-63.
Cho N.H., Lim S.Y., Kim Y.T., Kim D., Kim Y.S., Kim J.W. (2003): G2 checkpoint in uterine cervical cancer with HPV 16 E6 according to p53 polymorphism and its screening value. Gynecol Oncol. Jul;90(1):15-22.
Sauer S., Lechner D., Berlin K., Lehrach H., Escary J.L., Fox N., Gut I.G. (2000): A novel procedure for efficient genotyping of single nucleotide polymorphisms. Nucleic Acids Res. Mar 1;28(5):E13.
Protein dephosforylation
Crawley S.W., Gharaei M.S., Ye Q., Yang Y., Raveh B., London N., Schueler-Furman O., Jia Z., Côté G.P. (2011): Autophosphorylation activates Dictyostelium myosin II heavy chain kinase A by providing a ligand for an allosteric binding site in the alpha-kinase domain. J Biol Chem. Jan 28;286(4):2607-16. Epub 2010 Nov 11.
Mehta P.A., Rebala K.C., Venkataraman G., Parida A. (2009): A diurnally regulated dehydrin from Avicennia marina that shows nucleo-cytoplasmic localization and is phosphorylated by Casein kinase II in vitro. Plant Physiol Biochem. Aug;47(8):701-9. Epub 2009 Mar 28.
SAP for quantification
Wadler C., Cronan J.E. (2007): Dephospho-CoA kinase provides a rapid and sensitive radiochemical assay for coenzyme A and its thioesters. Anal Biochem. Sep 1;368(1):17-23. Epub 2007 Jun 7.
Donald C.E., Stokes P., O’Connor G., Woolford A.J. (2005): A comparison of enzymatic digestion for the quantitation of an oligonucleotide by liquid chromatography-isotope dilution mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci. Mar 25;817(2):173-82.
For pyrosequensing
Nordström T., Nourizad K., Ronaghi M., Nyrén P. (2000): Method enabling pyrosequencing on double-stranded DNA.
Anal Biochem. Jul 1;282(2):186-93.