Heliconema minnanensis n. sp. (Physalopteroidae: Physalopteridae) and Raphidascaris trichiuri (Yin and Zhang) n. comb. (Ascaridoidea: Anisakidae) in marine fishes.

Heliconema minnanensis n. sp. is described from the Chiloscyllium plagiosum south of the Minnan-Taiwan Bank Fishing Ground, Taiwan Strait. It is characterized by having the following combination of features. There are no longitudinal ridges in the posterior part of the body; the male has 4 pairs of precloacal papillae and 6-7 pairs of postcloacal papillae. The right spicule averages 0.2 mm long (1.1% of body length), and the left spicule averages 1.2 mm long (5.6% of body length), making an average spicule ratio of 1:5.2. The female has a vulva located on the left side of a thick membrane and 56-65% of the body length from the anterior end. Raphidascaris trichiuri (Yin and Zhang, 1983) comb. n., known previously from males only, is transferred from Cloeoascaris and redescribed, including material of both sexes from Muraenesox cinereus from the type locality.

Role of phosphate in Fe2+ binding to horse spleen holoferritin.

In order to identify the function and location of phosphate associated with the iron core of horse spleen ferritin (HoSF), the phosphate content of native HoSF was altered by two procedures. Adjustment of pH from 7.0 to 10.0 irreversibly released 53% of the phosphate and 10% of the iron, while lowering the pH to 5.0 reversibly released 43% of the phosphate and 35% of the iron. Reversible release of 85% of the initial phosphate (but little iron release) also occurs upon reduction with methyl viologen (MV) or dithionite. Most of the phosphate is released in the early stages of reduction of the iron core, suggesting that the phosphate resides primarily on the mineral core surface. Reduction followed by chelation altered both the iron and phosphate content of the HoSF mineral cores. HoSF iron cores first reconstituted in the absence of phosphate and then incubated with added phosphate did not bind phosphate. However, when HoSF was first reconstituted in the absence of phosphate and then equilibrated anaerobically with both Fe2+ and phosphate, then phosphate was incorporated in amounts similar to native HoSF. Fe2+ binding to native, phosphate altered, and reconstituted HoSF in the presence and absence of phosphate clearly showed that Fe2+ binding to the mineral core depends on the presence of core-bound phosphate. Fe2+ binding to phosphate-depleted mineral cores or to cores reconstituted with 621, 2158, and 3013 Fe/HoSF core in the absence of phosphate bound only eight Fe2+ per entire ferritin molecule, clearly showing that Fe2+ has no measurable affinity for the phosphate-free, reconstituted mineral core.(ABSTRACT TRUNCATED AT 250 WORDS)