. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 30 4O Time (minutes) Figure 2. The effect of coupons ( cm2) of chitosan (without cross- linked peptide or protein) and a peptide-chitosan complex (polyaspartate, MW 11,500, immobilized on chitosan by glutaraldehyde) on CaCO, crystallization. Error bars represent typical standard deviations (n = 3). promotion of crystal growth was observed with the washed decalcified carapace present compared to the nearly con- trol levels of crystal growth observed with the washed membranous layer present (Gunthorpe, 1989). Thus, loosely
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 30 4O Time (minutes) Figure 2. The effect of coupons ( cm2) of chitosan (without cross- linked peptide or protein) and a peptide-chitosan complex (polyaspartate, MW 11,500, immobilized on chitosan by glutaraldehyde) on CaCO, crystallization. Error bars represent typical standard deviations (n = 3). promotion of crystal growth was observed with the washed decalcified carapace present compared to the nearly con- trol levels of crystal growth observed with the washed membranous layer present (Gunthorpe, 1989). Thus, loosely associated protein in the crystal-promoting cou- pons may have diffused into the solution and inhibited crystal growth. Deposition of crystals was localized on insolubilized protein complexes, giving rise to a slow rate of crystallization that began significantly sooner than ob- served in controls. Suspensions of chitosan, a partially cationic surface at pH did not promote CaCO3 crystallization (Table III). Various immobilized peptide-chitosan complexes promoted crystallization (Table III; Fig. 2). The presence of an Alas tail on Asp:() showed suppression of promotion (P < ; balanced, incomplete block design), but this tail did not affect promotion when attached to Asp40 (Fig. 3). The quantities of the various peptides crosslinked to chitosan were statistically the same. Control solutions containing peptides but not chitosan coupons indicated a ± decrease in the amount of peptides (n = 3) due to interactions with glutaraldehyde after the cross- linking procedure. When the coupon was present, there was a to decrease in the amount of peptide left in the solution after 1 h. The larger peptides were crosslinked to chitosan to a lesser extent than were the smaller peptides. As also seen in the studies using the crab carapace sys- tem (Table II and Fig. 1), the rate of crystal growth was reduced when coupons with immobilized peptides were suspended in
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Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
