%0 Journal Article %1 Varum1997a %A Varum, K. M. %A Myhr, M. M. %A Hjerde, R. J. N. %A Smidsrod, O. %C THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD, OXON, ENGLAND OX5 1GB %D 1997 %I ELSEVIER SCI LTD %J Carbohydr. Res. %K ; ;; [ISI:] chitinase chitins chitosan; chitosans; deacetylated degradation; field lysozyme; nmr-spectroscopy serum; %N 1-2 %P 99 -- 101 %T In vitro degradation rates of partially N-acetylated chitosans in human serum %V 299 %X The initial degradation rates (r) in human serum of three chitosans with F-A = 0.42, 0.51, and 0.60 were determined by measuring the decrease in viscosity as a function of time. A strong increase in r with increasing F, of the chitosans was observed, with r increasing proportionally to F-A(4.5). With increasing concentrations of lysozyme added to the reaction mixtures of chitosan and serum, the relative increase in degradation rate of chitosans with increasing F-A was almost the same as that without lysozyme added. Addition of the chitinase inhibitor allosamidin (50 mu M) did not inhibit the degradation rate of chitosan (F-A = 0.60) by human serum. The results suggest that chitosans are actually mainly depolymerized by lysozyme in human serum, and not by other enzymes or other depolymerization mechanisms. (C) 1997 Elsevier Science Ltd.

@article{Varum1997a, __markedentry = {[phpts:6]}, abstract = {The initial degradation rates (r) in human serum of three chitosans with F-A = 0.42, 0.51, and 0.60 were determined by measuring the decrease in viscosity as a function of time. A strong increase in r with increasing F, of the chitosans was observed, with r increasing proportionally to F-A(4.5). With increasing concentrations of lysozyme added to the reaction mixtures of chitosan and serum, the relative increase in degradation rate of chitosans with increasing F-A was almost the same as that without lysozyme added. Addition of the chitinase inhibitor allosamidin (50 mu M) did not inhibit the degradation rate of chitosan (F-A = 0.60) by human serum. The results suggest that chitosans are actually mainly depolymerized by lysozyme in human serum, and not by other enzymes or other depolymerization mechanisms. (C) 1997 Elsevier Science Ltd.}, added-at = {2011-11-04T13:47:04.000+0100}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD, OXON, ENGLAND OX5 1GB}, author = {Varum, K. M. and Myhr, M. M. and Hjerde, R. J. N. and Smidsrod, O.}, biburl = {https://www.bibsonomy.org/bibtex/23a0655a59a54e97ef62e1e50986faf27/pawelsikorski}, citedref = {ANTHONSEN MW, 1993, CARBOHYD POLYM, V22, P193 ; DRAGET KI, 1992, BIOMATERIALS, V13, P635 ; ESCOTT GM, 1995, INFECT IMMUN, V63, P4770 ; KOGA D, 1987, AGR BIOL CHEM TOKYO, V51, P471 ; NORDTVEIT RJ, 1994, CARBOHYD POLYM, V23, P253 ; NORDTVEIT RJ, 1996, CARBOHYD POLYM, V29, P163 ; OVERDIJK B, 1994, GLYCOBIOLOGY, V4, P797 ; RENKEMA GH, 1995, J BIOL CHEM, V270, P26252 ; SANNAN T, 1976, MAKROMOL CHEM, V177, P3589 ; STOKKE BT, 1995, CAN J CHEM, V73, P1972 ; VARUM KM, 1991, CARBOHYD RES, V211, P17 ; VARUM KM, 1991, CARBOHYD RES, V217, P19 ; VARUM KM, 1996, BBA-GEN SUBJECTS, V1291, P5}, interhash = {db9f14739e073661e6a733f737b73f73}, intrahash = {3a0655a59a54e97ef62e1e50986faf27}, isifile-dt = {Article}, isifile-ga = {WT993}, isifile-j9 = {CARBOHYD RES}, isifile-nr = {13}, isifile-pi = {OXFORD}, isifile-rp = {Varum, KM, NORWEGIAN UNIV SCI & TECHNOL,DEPT BIOTECHNOL,NOBIPOL,N-7034 ; TRONDHEIM,NORWAY.}, isifile-sc = {Biochemistry & Molecular Biology; Chemistry, Applied; Chemistry, Organic}, isifile-tc = {24}, issn = {0008-6215}, journal = {Carbohydr. Res.}, keywords = {; ;; [ISI:] chitinase chitins chitosan; chitosans; deacetylated degradation; field lysozyme; nmr-spectroscopy serum;}, language = {English}, month = {MAR 26}, number = {1-2}, owner = {phpts}, pages = {99 -- 101}, publisher = {ELSEVIER SCI LTD}, size = {3 p.}, sourceid = {ISI:A1997WT99300013}, timestamp = {2011-11-04T13:47:27.000+0100}, title = {In vitro degradation rates of partially N-acetylated chitosans in human serum}, volume = 299, year = 1997 }