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Solubilization, Activation and Partial Purification of A Sialidase from Horse Liver
Oleh:
Schauer, Roland
;
Roggentin, Peter
;
Candra, Krishna Purnawan
Jenis:
Article from Journal - ilmiah nasional - terakreditasi DIKTI
Dalam koleksi:
Hayati Journal of Biosciences vol. 12 no. 3 (Sep. 2005)
,
page 87-92.
Topik:
AIR - PURIFICATION - EQUIPMENT AND SUPPLIES
;
Horse Liver
;
Sialidase
Fulltext:
46.pdf
(290.67KB)
Ketersediaan
Perpustakaan Pusat (Semanggi)
Nomor Panggil:
HH13.7
Non-tandon:
1 (dapat dipinjam: 0)
Tandon:
tidak ada
Lihat Detail Induk
Isi artikel
Using sialyl-methylumbelliferyl a-glycoside as substrate, sialidase in horse liver was detected as a membrane-bound enzyme. A yield about 50% of sialiside activity was found in supernatant when solubilized in 0.1 M sodium-phospate buffer pH 5.5, containing 0.15 M NaCl, 0.25 M sucrose, and 0.5% Triton X-100. Sialidase in the solubilisate could be activated by incubating in adicid pH at 37 celcius degree. Incubation of this solubilized enzyme at 37 celcius degree for 1.5 h at pH 5.0 led to 10% increase of activity and to the precipitation of about 50% of contamining protein. Using cation-exchange chromatography on S-Sepharose FF and affinity chromatography on p-aminophenyl oxamic acid-agarose following solubilization and activation, about 6% of total sialidase activity was recovered with the purification factor of about 500. The pH and temperature optimum were measured at pH 4.3 and between 37-45 celcius degree, respectively. Neu5Ac2en was a strong inhibitor, while p-aminophenyl oxamic acid had only a weak inhibitory effect.
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