. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. Pink 280 nm B 160 0) I 120 | .-•' Brown 280 nm o Pink 560 nm !£ 80 O P 40 Brown 560 nm. 26 27 28 Elution Time (min) -60 -30 0 30 60 Area of 280 slice Figure 4. Relationship between absorbance at 560 nm and 280 nm. (A) Chromatograms of phosphate buffer extracts from pink and brown branches of Pocilloporu damicurnis: shaded slices show area used in 280 determination. (B) Linear relationship between area of 560 slice and area of 280 slice: r = ; (•) colony 1: (O) colony 2. between the 560-nm absorption and 280-nm absorption
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. Pink 280 nm B 160 0) I 120 | .-•' Brown 280 nm o Pink 560 nm !£ 80 O P 40 Brown 560 nm. 26 27 28 Elution Time (min) -60 -30 0 30 60 Area of 280 slice Figure 4. Relationship between absorbance at 560 nm and 280 nm. (A) Chromatograms of phosphate buffer extracts from pink and brown branches of Pocilloporu damicurnis: shaded slices show area used in 280 determination. (B) Linear relationship between area of 560 slice and area of 280 slice: r = ; (•) colony 1: (O) colony 2. between the 560-nm absorption and 280-nm absorption (Fig. 4B: linear relation with r2 = ). Extinction coefficient. The extinction coefficient (t560) of pocilloporin was determined directly from three in- dependent chromatograms of purified pocilloporin ( Fig. 1 A) and was 34059 ± 1635cm"1 A/"'(mean ± SEM). The extinction coefficient measured using a spectropho- tometer applied to purified protein from five HPLC runs was 31950 cm ' A/"1 (using the method of Whitaker and Granum, 1980, to measure protein) and 32900 cirT1 M~[ (using the method of Bradford, 1976. to measure protein). The three methods resulted in extinction coefficients for pocilloporin that were not statistically different (P> ), hence verifying the validity of the first method. Metal ion analysis. The association of metal ions with pocilloporin was investigated using ICP-MS. Total-quant analysis of the ion content of pocilloporin samples re- vealed no ions occurring at significantly greater levels than background; therefore, pocilloporin does not have an ac- companying metal ion in its structure. Thermal lability of pocilloporin. Chromatograms at 280 nm and 560 nm of pocilloporin from a broad collec- tion around 560 nm are asymmetrical (Fig. 5A), dem- onstrating that the fraction (in this case) was contaminated with proteins other than pocilloporin. No changes occured to pocilloporin when it was heated to 40°C for 10 min. Whe
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Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
