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dc.contributor.authorCandra, Krishna Purnawan
dc.date.accessioned2019-10-19T03:08:50Z
dc.date.available2019-10-19T03:08:50Z
dc.date.issued2006
dc.identifier.issn979-99675-1-1
dc.identifier.urihttp://repository-ds.unmul.ac.id:8080/handle/123456789/984
dc.description.abstract“Different” sialidases from partially purification of two kinds of horse liver was studied to find out the catabolism of 4-O-acetylated N-acetylneuraminic acid (Neu4,5Ac2) with guinea pig serum as substrate. Using fluorimetric HPLC as tools to determine the free sialic acid released from the natural substrate, there was no Neu4,5Ac2 released by the sialidase detected. This data emphasize that esterase was involved in the released of Neu4,5Ac2 from sialoglycoconjugate.
dc.publisherASEAN Biochemistry Seminar, Enzymes: Industrial and Medical Prospects, Surabaya, February 6-7, 2006.
dc.titleCatabolism of 4-O-Acetylated Sialic Acid


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