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Alkaline phosphatase purification

E6. Engstrom, L., Studies on bovine-liver alkaline phosphatase, purification, phosphate incorporation. Biochim. Biophys. Acta 92, 71-78 (1964). [Pg.353]

Preparation of specific antisera against adeno- 136 viruses by affinity bead immunization Development of an immunoadsorbent method 137 for the continuous purification of human placental alkaline phosphatase Purification by immunoadsorption of a-amylase 138 inhibitor from P. vulgaris... [Pg.594]

Purification of the steroid-active isoenzyme of alcohol dehydrogenase by affinity chromatography Isolation of ribonucleotide reductase by affinity chromatography Investigations of the effects of different spacer arms on the affinity chromatography of alkaline phosphatase Purification of P-450 haemeproteins of Rhizobium japonicum by affinity chromatography... [Pg.438]

Biomedical Applications. TRIS AMINO is used for a number of purposes in its pure form, it is an acidimetric standard the USP grade can be utilized intraveneously for therapeutic control of blood acidosis TRIS AMINO also is useful in genetic engineering as a buffering agent for enzyme systems, industrial protein purification, and electrophoresis. AMP has found use as a reagent in enzyme-linked immunoassays. The primary appHcation is for alkaline phosphatase assays. [Pg.19]

Farmer, J.C., and Castaneda, M. (1991) An improved preparation and purification of oligonucleotide-alkaline phosphatase conjugates. Bio. Tech. 11, 588-589. [Pg.1062]

Isolation and characterization. Alkaline phosphatase is concentrated in the fat globule membrane and hence in cream. It is released into the buttermilk on phase inversion consequently, buttermilk is the starting material for most published methods for the purification of alkaline phosphatase. Later methods have used chromatography on various media to give a homogeneous preparation with 7440-fold purification and 28% yield. The characteristics of milk alkaline phosphatase are summarized in Table 8.2. The enzyme appears to be similar to the alkaline phosphatase of mammary tissue. [Pg.243]

Dunn, B. E., Edberg, S. C., and Torres, A. R. (1988). Purification of E. coli alkaline phosphatase on an ion-exchange HPLC column using carboxymethyl dextrans. Anal. Biochem. 168, 25-30. [Pg.413]

Fig. 8. Relationship between pX versus pH for intestine (rat) and placental (human) alkaline phosphatases. Filled circles represent intestine and open triangles human placenta. The plot for intestinal enzyme is made according to Ghosh and Fishman (G5). Ammonium sulfate fractionation was omitted during the purification of the placental enzyme. Fig. 8. Relationship between pX versus pH for intestine (rat) and placental (human) alkaline phosphatases. Filled circles represent intestine and open triangles human placenta. The plot for intestinal enzyme is made according to Ghosh and Fishman (G5). Ammonium sulfate fractionation was omitted during the purification of the placental enzyme.
Previous work on human alkaline phosphatases has utilized chromatography (ElO) and starch-gel electrophoresis. Thus in 1956 Boman and Westlund (B34) reported the purification and separation of serum phosphatases by Dowex-2 column chromatography. Moss (M34) used gel filtration on Sephadex G-200 and DEAE-celluIose chromatography for separating 5 -nucleotidase and nonspecific alkaline phosphatase activities in human sera. In most of the studies of alkaline phosphatases in human tissues of liver (M33), intestine (M34, M35), bone (M36), kidney (B46), and urine (B44, B46, B47), crude extracts of these tissues were used and... [Pg.293]

Pio. 18. Starch-gel pattern of placental alkaline phosphatase isozymes in the final steps of the purification (a) variant A and B in the best alcohol fractions before Sephadex-gel filtration, (b) variant A after removing B in the Sephadex-gel column, and (c) crystalline alkaline phosphatase (variant B). [Pg.294]

A4. Ahmed, Z., and King, E. J., Purification of placental alkaline phosphatase. Biochim. Biophys. Acta iO, 320-328 (1960). [Pg.348]

A16. Anagnostopoulos, C., and Matsudaira, H., Purification and kinetic studies of the alkaline phosphatase of human placenta. Proc. Intern. Symp. Enzyme Chtm., Tokyo Kyoto, 1957 (K. Ichihara, ed.), p. 166. Manizen, Tokyo, 1958. [Pg.348]

Dl. Dabich, D., and Neuhas, O. W., Purification and properties of bovine synovial fiuid alkaline phosphatase. J. Biol. Chem. 241, 415-420 (1966). [Pg.352]

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See also in sourсe #XX -- [ Pg.815 ]

See also in sourсe #XX -- [ Pg.377 ]

See also in sourсe #XX -- [ Pg.377 ]

See also in sourсe #XX -- [ Pg.377 ]

See also in sourсe #XX -- [ Pg.194 ]



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