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Results: 1-4 |
Results: 4
N-TERMINAL STRETCH ARG(2), ARG(3), ARG(4) AND ARG(5) OF HUMAN LACTOFERRIN IS ESSENTIAL FOR BINDING TO HEPARIN, BACTERIAL LIPOPOLYSACCHARIDE, HUMAN LYSOZYME AND DNA
Authors: VANBERKEL PHC GEERTS MEJ VANVEEN HA MERICSKAY M DEBOER HA NUIJENS JH
Citation: Phc. Vanberkel et al., N-TERMINAL STRETCH ARG(2), ARG(3), ARG(4) AND ARG(5) OF HUMAN LACTOFERRIN IS ESSENTIAL FOR BINDING TO HEPARIN, BACTERIAL LIPOPOLYSACCHARIDE, HUMAN LYSOZYME AND DNA, Biochemical journal, 328, 1997, pp. 145-151
CHARACTERIZATION OF RECOMBINANT HUMAN LACTOFERRIN SECRETED IN MILK OFTRANSGENIC MICE
Authors: NUIJENS JH VANBERKEL PHC GEERTS MEJ HARTEVELT PP DEBOER HA VANVEEN HA PIEPER FR
Citation: Jh. Nuijens et al., CHARACTERIZATION OF RECOMBINANT HUMAN LACTOFERRIN SECRETED IN MILK OFTRANSGENIC MICE, The Journal of biological chemistry, 272(13), 1997, pp. 8802-8807
HETEROGENEITY IN UTILIZATION OF N-GLYCOSYLATION SITES ASN(624) AND ASN(138) IN HUMAN LACTOFERRIN - A STUDY WITH GLYCOSYLATION-SITE MUTANTS
Authors: VANBERKEL PHC VANVEEN HA GEERTS MEJ DEBOER HA NUIJENS JH
Citation: Phc. Vanberkel et al., HETEROGENEITY IN UTILIZATION OF N-GLYCOSYLATION SITES ASN(624) AND ASN(138) IN HUMAN LACTOFERRIN - A STUDY WITH GLYCOSYLATION-SITE MUTANTS, Biochemical journal, 319, 1996, pp. 117-122
GLYCOSYLATED AND UNGLYCOSYLATED HUMAN LACTOFERRINS BOTH BIND IRON ANDSHOW IDENTICAL AFFINITIES TOWARDS HUMAN LYSOZYME AND BACTERIAL LIPOPOLYSACCHARIDE, BUT DIFFER IN THEIR SUSCEPTIBILITIES TOWARDS TRYPTIC PROTEOLYSIS
Authors: VANBERKEL PHC GEERTS MEJ VANVEEN HA KOOIMAN PM PIEPER FR DEBOER HA NUIJENS JH
Citation: Phc. Vanberkel et al., GLYCOSYLATED AND UNGLYCOSYLATED HUMAN LACTOFERRINS BOTH BIND IRON ANDSHOW IDENTICAL AFFINITIES TOWARDS HUMAN LYSOZYME AND BACTERIAL LIPOPOLYSACCHARIDE, BUT DIFFER IN THEIR SUSCEPTIBILITIES TOWARDS TRYPTIC PROTEOLYSIS, Biochemical journal, 312, 1995, pp. 107-114
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