. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. METACERCARIA HEMOGLOBIN Tabic I C '< imparison of absorption maxima (run) for metacercaria, Amphitnte ornata and human hemoglobins1' 175 Amphitrite ornata Metacercaria Vascular Coelomic Human OXY Of () () () () 0 () () () () 7 () () () () DEOXY afi () () () () 7 () (-/I) () () CARBOXY a 569** 570** () * 0 538*
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. METACERCARIA HEMOGLOBIN Tabic I C '< imparison of absorption maxima (run) for metacercaria, Amphitnte ornata and human hemoglobins1' 175 Amphitrite ornata Metacercaria Vascular Coelomic Human OXY Of () () () () 0 () () () () 7 () () () () DEOXY afi () () () () 7 () (-/I) () () CARBOXY a 569** 570** () * 0 538** 538** () 539* t 421** 421** () 420* Data are from Van Assendelft (1970). * Data are from Chiancone elal. (1980). ' The numbers in parentheses represent standard deviation/number of samples. samples (see above for conditions). Sequential one-half ml fractions of the entire gel filtration eluent were col- lected and the amount of label in each determined using a Beckman LS7000 Liquid Scintillation Counter. Results /// vivo spectrophotometry of metacercaria tissues showed characteristic hemoglobin spectra when the tis- sues were exposed to oxygen, nitrogen, and carbon mon- oxide. The in vivo absorption spectra for metacercaria hemoglobin are shown in Figure 1. The absorption max- ima of metacercaria tissue hemoglobin and Amphitrite ornata HMW and coelomic cell hemoglobins are listed in Table I along with the maxima for human hemoglo- bin. Only minor variations in maxima are apparent be- tween all four pigments. Absorption spectra of metacer- caria gut contents gave absorption profiles that were not recognizable as typical for hemoglobin in oxy, deoxy, or met state (Van Assendelft, 1970). Oxygen equilibrium curves for metacercaria hemoglo- bin in vivo are shown in Figure 2. The in vivo oxygen binding properties of metacercaria hemoglobin are sum- marized in Table II. The hemoglobin has a high affinity for oxygen and demonstrates cooperative oxygen bind- ing. I
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Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
