|Budget Amount *help
¥1,700,000 (Direct Cost : ¥1,700,000)
Fiscal Year 1994 : ¥400,000 (Direct Cost : ¥400,000)
Fiscal Year 1993 : ¥1,300,000 (Direct Cost : ¥1,300,000)
Glycosaminoglycans (GAGs), which are located predominantly on the cell surface or in the extracellular matrix, are of particular interest in important biological phenomena such as cell adhesion, cell growth, and cancer metastasis. An understanding of these biological processes is intimately linked to a knowledge of the structures involved. However, compared with the progress achieved in structural analysis of other biopolymers such as proteins and nucleic acids, Progress has been rether slow in the field of GAGs. Therefore, we aim to develop new techniques for releasing intact GAG chains from proteoglycans and for analyzing their primary structure. For the former purpose, we found some GAG-degrading endoglycosidases, for example, endo-beta-glucuronidase, endo-beta-xylosidase, and endo-beta-galactosidase, corresponding to the restriction enzymes which act on DNA.Also, it is known that glycosidases catalyse not only hydrolysis but also transglycosylation. Therefore, we applied the transglycosylation activity of these endoglycosidases to reconstrust various GAGs which have biological activities. For the latter purpose, we used ion-spray mass spectrometry-tandem mass spectrometry (IS-MS/MS) to analysis of primary structure. Advances in these techniques are strongly expected to speed up the progress of research in "glycotechnology".