FAB MASS SPECTROMETRY OF HUMAN FIBRINOGENS.

D. Heller, C. Fenselau, R. Townsend, Y. C. Lee

Research output: Contribution to journalConference articlepeer-review

Abstract

Total desialylation of most glycoproteins results in their removal from circulation within minutes by the liver. Asialo triantennary oligosaccharides are implicated as a major determinant of this clearance (i. e. , exposure of galactose residues). Human fibrinogen, possessing only biantennary oligo-saccharides, is cleared over hours, however. Since isolated fibronogen is partially desialylated, it becomes important to characterize the sialylation pattern of isolated native fibrinogen, and eventually to determine the clearance rate of fibrinogen possessing a defined array of sialic acid residues. Towards this end, a method of determining relative proportions of sialic acid-containing oligosaccharides by positive FAB mass spectrometry was investigated, with the goal to relate relative intensity of molecular ion peaks to the relative proportion of each species in a mixture.

Original languageEnglish
Pages (from-to)339-340
Number of pages2
JournalAnnual Conference on Mass Spectrometry and Allied Topics
StatePublished - Dec 1 1984
Externally publishedYes

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