Placenta purification

Blackburn, P., G. Wilson, and S. Moore. 1977. Ribonuclease inhibitor from human placenta Purification and properties. J Biol Chem 252 5904. 

Purification of glycosulphatase Purification of horseradish peroxidase Purification of human-liver p-D-galactosidasei Purification of P-D-2-acetamido-2-deoxy-hexosidases A and B from human placenta Purification of pepsin glycopeptides from human immunoglobulin IgAj myeloma glycoprotein... 

HSA is used therapeutically as an aqueous solution it is available in concentrated form (15-25 per cent protein) or as an isotonic solution (4-5 per cent protein). In both cases, in excess of 95 per cent of the protein present is albumin. It can be prepared by fractionation from normal plasma or serum, or purified from placentas. The source material must first be screened for the presence of indicator pathogens. After purification, a suitable stabilizer (often sodium caprylate) is added, but no preservative. The solution is then sterilized by filtration and aseptically filled into final sterile containers. The relative heat stability of HSA allows a measure of subsequent heat treatment, which further reduces the risk of accidental transmission of viable pathogens (particularly viruses). This treatment normally entails heating the product to 60 °C for 10 h. It is then normally incubated at 30-32 °C for a further 14 days and subsequently examined for any signs of microbial growth. 

H.J. Kliman, J.E. Nestler, E. Sermasi, J.M. Sanger, and J.F. Strauss, III. Purification, characterization, and in vitro differentiation of cytotrophoblasts from human term placentae. Endocrinology. 118 1567-1582 (1986). 

Acid CDase was first described by Gatt (1963, 1966) in rat brain. The enzyme was found to have a pH optimum of 5, to be independent of MgCl2, CaCl2 and MnCl2, and the molecular mass was estimated to be -150 kDa. Three years latter, the same group reported a 200-fold purification of the enzyme from the 27,000 x g membranes of rat brains (Yavin and Gatt, 1969). Subsequently, acid CDase was partially purified from human placenta 300-fold by Chen et al. (1981). The purified enzyme had a pH optimum similar to that obtained from rat brain, but the molecular mass was estimated to be -47 KDa. 

Ramamoorthy S, Leibach FH, Mahesh VB, Ganapathy V (1993) Partial purification and characterization of the human placental serotonin transporter. Placenta 14 449-461 Rasmussen BB, Brosen K (2000) Is therapeutic drug monitoring a case for optimizing clinical outcome and avoiding interactions of the selective serotonin reuptake inhibitors Ther DrugMonit 22 143-154... 

Tilgmann C, Kalkkinen N. Purification and partial sequence analysis of the soluble catechol-Cometh 1 transferase from human placenta Comparison to the rat liver enzyme. Biochemical and Biophysical Research Communications 1991 174 995-1002. 

Tamiya, N. Yusa, T. Yamaguchi, Y Tsukifuji, R. Kuroiwa, N. Moriyama, Y. Fujimura, S. Co-purification of thymidylate kinase and cytosolic thymidine kinase from human term placenta by affinity chromatography. Biochim. Biophys. Acta, 995, 28-35 (1989)... 

Mbida, A. D., Kanoun, S., and Vijayalakshmi, M. A. (1989). Purification of IgGl subclass from human placenta by pseudoaffinity chromatography. In Biotechnology of Plasma Proteins, Vol. 175, pp. 237-243. INSERM, Paris. 

Also N. K. Tbriks, C. D. Diltz and E. H. Fischer, Purification of the major protein-tyrosine-phosphatases of human placenta. J. Bid. Chem. 263, 6722-6730. 1988... 

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.

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. 

B24. Bhaumick, B., Bala, R. M., and Hollenberg, M. D., Somatomedin receptor (ff human placenta Solubilization, photolabeling, partial purification, and comparison with insulin receptor. Proc. Nad. Acad. Sci. U S.A. 78, 4278-4283 (1981). 

Oppenheimer, C. L., and Czech, M. P., Purification of the type II insulin-lil growth factor receptor from rat placenta. J. Biol. Chem. 258, 8539-8542 (1983). 

Ferritin (from human placenta) [9007-73-2] Mr 445,000 (Fe free protein). The purification... 

Farooqui, A. A., Purification and properties of human placenta arylsulfatase A. Arch. Int. Physiol. Biochim. 84, 479-492 (1976a). 

ClossI, J., Truppe, W., and Kresse, H., Purification and properties of N-acetylgalactosamine 6-sulfate sulfatase from human placenta. Biochem.. 181, 37—46 (1979). 

Gniot-Szulzycka, J., Human placenta arylsulfatase B Purification and separation into subfractions. Acta Biochim. Pol. 19, 181-189 (1972). 

G13. Guthenberg, C., Akerfeldt, K., and Mannervik, B., Purification of glutathione S-transferase from human placenta. Acta Chem. Scand., Ser. B B33, 595-596 (1979). 

H52. Howie, A. F., Hayes, J. D., and Beckett, G. J., Purification of acidic glutathione S-transferases from human lung, placenta and erythrocyte and the development of a specific radioimmunoassay for their measurement. Clin. Chim. Acta 177, 65-76 (1988). 

P-Galactosidase. Lysosomal P-galactosidase can be purified from human liver or placenta with conventional methods (Meisler, 1972 Sloan, 1972 Miyatake and Suzuki, 1975) or with affinity chromatography on immobilized />-aminophenyl- or 6-aminohexyl-thio-3-D-galactoside (Miller et al., 1977 Lo et al., 1979). The most rapid and convenient procedure seems to be the two-step method of Miller et al. (1977), which is reported to give a more than 20,000-fold purification with 41% yield. The affinity gel is commercially available. 

Arylsulfatase A. As noted before, the arylsulfatase A preparations used for assays with sulfatide and the natural activator protein have to be rather pure since contaminating proteins may interfere with this reaction in vitro. A variety of methods have been published for purification of the enzyme from human liver (Draper et al., 1976 James and Austin, 1979), kidney (Stinshoff, 1972), placenta (Gniot-Szulzycka and Komoszynski, 1970), and urine (Breslow and Sloan, 1972 Stevens et al., 1975). In our laboratory the procedure of Stinshoff (1972) is usually followed. 

Three papers have appeared on the isolation and purification of the 2-deoxy-D-glucoside-2-sulphamate sulphohydrolase (128) from liver174-176. The enzyme has been purified 40,000-fold utilizing four chromatographic steps. The purification procedures were followed using a specific substrate isolated from an acid hydrolysate of heparin. The subunit molecular weight (Mr) of the enzyme isolated from liver, kidney and placenta was assessed to be 56,000 using SDS/polyacrylamide-gel electrophoresis and the native enzyme results from the dimerisation of the subunits. 

Human indoleamine 2,3-dioxygenase is most abundant in the placenta, followed by the lung and small intestine (15). Even in the placenta, however, the content (0.25 nmobmin -mg of protein) is about 5% of that (5.6 nmol-min mg of protein) in rabbit intestine, and a 10,000-fold purification is required, starting from the crude extract of the placenta. 

Purification of Indoleamine 2,3-Dioxygenase from Human Placenta... 

Sarkar P, Bhatacharya P, Mukherjea R (1987) Isolation and purification of protease from human placenta by foam fractionation. Biotechnol Bioeng 29 934-940 Savidge T (1984) Enzymatic conversions used in the production of penidUins and cephalosporins. In Vandamme E (ed). Biotechnology of industrial antibiotics. Marcel Dekker, New York, pp 171-224... 

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