Red abalone

Anderlini, V. 1974. The distribution of heavy metals in the red abalone, Haliotis rufescens, on the California coast. Arch. Environ. Contam. Toxicol. 2 253-265. 

United Kingdom shell vs. soft parts Red abalone, Haliotis rufescens California ... 

Hunt, J.W. and B.S. Anderson. 1989. Sublethal effects of zinc and municipal effluents on larvae of the red abalone Haliotis rufescens. Mar. Biol. 101 545-552. 

Fig. 2. Nacre of red abalone shell Halitotis refescens), imaged here by transmission electron microscopy (left), has a bricks-and-mortar structure. The bricks are CaCOs (aragonite) platelets, and the mortar is a composite of macromolecules, including structural proteins and polysaccharides, that form a thin film around the platelets. The three-dimensional structure is depicted on the right [23]...

Winter, F.C. and Estes, J.A., Experimental evidence for the effects of polyphenolic compounds from Dictyoneurum califomicum Ruprecht (Phaeophyta Laminariales) on feeding rate and growth in the red abalone Haliotus rufescens Swainson, J. Exp. Mar. Biol. Ecol., 155, 263, 1992. 

Slattery, M., Larval settlement and juvenile survival in the red abalone (Haliotis rufescens) an examination of inductive cues and substrate selection, Aquaculture, 102, 143, 1992. 

Barlow, L. A., Electrophysiological and behavioral responses of larvae of the red abalone (Haliotis rufescens) to settlement-inducing substances, Bull. Mar. Sci., 46, 537, 1990. 

More recently, an abalone sperm attractant has been identified. Sperm of the red abalone Haliotis rufescens responds to soluble factors released into the seawater by conspecific eggs. Bioassay-guided purification revealed... 

Figure 1. An unfertilized egg of the red abalone Haliotis rufescens. The dark egg is 1 75 l m in diameter. The vitelline envelope is 0.6 pm in thickness and 245 pm in diameter (from Lewis et al., 1982).

Figure 7. Species-specific dissolution of isolated VEs by purified lysins as determined by the light scattering assay. Vertical axis, percent VE dissolved horizontal axis, qg lysin added. R j, VEs from the red abalone, H. rufescens. B j, VEs from the black abalone, H. cracherodii. Pyj, VEs from the pink abalone, H. corrugata. ( ) red lysin (A) pink lysin and ( ) black lysin (from Vacquier and Lee, 1993).

Figure 8. The fusion of artificial phospholipid vesicles induced by 18K protein (a) and lysin (b) at the three concentrations indicated above (c, buffer alone). The upper panels are with sperm proteins from the red abalone (Hr H. refescens) the lower panels are with sperm proteins from the green abalone (Hf H. fulgens). The 18K proteins are more potent fusagens than lysin. Although the two 18K proteins are only 33.8% identical in primary structure, their five predicted amphipathic helices have similar hydrophobic moments (from Swanson and Vacquier, 1995a).

Figure 11. The crystal structure of the red abalone lysin monomer. The a-carbon trace shows the five a-helices numbered a-1 to a-5 and the two basic tracks of Arg and Lys residues. The left basic track contains nine residues and the right track 14 residues (Arg and Lys are not visible in the crystal structure). The two termini are labeled N and C. The N-terminal segment of residues 1 to 12 extends away from the helical bundle and the hypervariable N- and C- termini are in proximity (from Shaw et al., 1993). In the Arg and Lys side chains, carbon atoms are white and nitrogen atoms dark gray.

Figure 75. Alignment of lysin and 18K proteins from red abalone. Both proteins have five exons (numbered) and four introns (positions shown by arrows). The position of intron three in lysin could not be determined and is shown by a question mark corresponding to the third 18K intron. For both proteins, the known introns are in the exact same positions and have the same phase in the interrupted codon (phase numbered above arrow head). These data indicate the two proteins arose by gene duplication.

Baginsky, M.L., Stout, C D., and Vacquier, V.D. (1990). Diffraction quality crystals of lysin from spermatozoa of the red abalone (Haliotis rufescens). J. Biol. Chem. 265 4958-4962. 

Diller, T.C., Shaw, A., Stura, E.A., Vacquier, V.D., and Stout, C.D. (1994). Acid pH crystallization of the basic protein lysin from the spermatozoa of red abalone Haliotis rufescens). Acta Crystallog., Sect. D 50 620-627. 

Heteronemin (178), first isolated from the sponge Heteromma erecta [175], was toxic to A. salina and gametes of the giant kelp Macrocystis pyrifera at 10 pg/ml and also immobilised the larvae of the red abalone Haliotis rufescens at 1 pg/ml [22]. Furthermore, heteronemin showed antituberculosis activity, inhibiting the growth of Mycobacterium tuberculosis with an MIC of 6.25 pg/ml [176]. Salmahyrtisol B (179), isolated from the Red Sea Hyrtios erecta [177], is related to scalarafiiran... 

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