Albert C. Smith

Variation in protein composition of the eye lens nucleus in ocean whitefish, Caulolatilus princeps

Abstract 1. 1. Protein from the nucleus of the eye lens in ocean whitefish was analyzed by a modified method of cellulose acetate electrophoresis. Distilled water and physiological saline were used to extract the protein. 2. 2. Fifty fish were caught at Cedros Island, Baja California, and nine at the Coronados Islands, near southern California. Fish of both regions produced two protein patterns in common, while fish from Cedros Island produced two additional patterns. 3. 3. The uniformity of the patterns in fish living 500 miles apart clearly demonstrates the reliability of the electrophoretic method. The presence of extra protein patterns in fish from Cedros Island indicates that electrophoresis of nuclear lens protein can be used to identify separate breeding populations. 4. 4. This method (electrophoresis of nuclear lens protein) effectively identifies molecular differences that reflect genetic variation between individuals of the same species.

Protein variation in the eye lens nucleus of the mackerel scad (Decapterus pinnulatus)

Abstract 1. 1. Electrophoretic patterns were prepared from mackerel scad (Decapterus pinnulatus) nuclear eye lens protein extracted in 0·018 g% NaCl solution. 2. 2. Sixteen fish from Hawaii and sixteen from Kauai, islands 300 miles apart, produced two protein patterns in common. Kauai fish produced two additional patterns, suggesting separate breeding populations of different sizes. 3. 3. The uniformity of many patterns demonstrates the reliability of the electrophoretic procedure and the genetic basis of the patterns. 4. 4. Low molecular weight nuclear lens proteins vary intraspecifically, permitting identification of separate breeding populations. High molecular weight proteins are less variable; consequently, they should be particularly useful in systematics research.

Effects of sodium chloride concentration on solubility and electrophoretic characteristics of protein from the eye lens nucleus in a yellowfin tuna (Thunnus albacares) and in a desert wood rat (Neotoma lepida).

Abstract 1. 1. A medium was sought which would extract from the eye lens nucleus all classes of proteins; albumins, euglobulins and pseudoglobulins. 2. 2. Cellulose acetate electrophoresis was performed on distilled water extracts and on saline extracts of thirty-three pieces of lens nucleus from a Yellowfin tuna, and of five pieces of lens nucleus from a desert wood rat. 3. 3. The protein patterns revealed that a 0·018 g% saline solution extracts both albumins and globulins, and produces no deleterious “salt effects”. The patterns also demonstrated that stronger saline solutions (e.g. physiological saline solution) produce simpler patterns due to the fusion of some proteins into single bands and the exclusion of others from solution. 4. 4. Of the various extracting fluids studied, the most effective for nuclear lens proteins, is 0·018 g% saline solution. Extracts prepared with this solution contain a total salt concentration of approximately 0·030 g% due to the presence of sodium chloride in the lens.

Electrophoretic, solubility and thermostability differences in proteins of eye lens nuclei from two closely related fish species, the yellowfin tuna and the bigeye tuna

Abstract 1. 1. Electrophoretic separation of protein from lens nuclei of yellowfin and bigeye tunas produced species-specific patterns. 2. 2. Certain of these proteins from the yellowfin and bigeye had identical electrophoretic mobilities but differed in solubility. 3. 3. In both tuna species, proteins from heated extracts revealed an increasing thermostability with increasing electrophoretic mobility and molecular weight. Proteins of bigeye, however, were more heat-stable than those of yellowfin. 4. 4. The electrophoretic, solubility and thermostability data indicate that the low molecular weight nuclear lens proteins are less alike than those of high molecular weight in related species.

Intraspecific variation in the soluble nuclear eye lens proteins of the sandbar shark, Carcharhinus Milberti (Müller and Henle)

Abstract 1. 1. The technique for studying genitically based molecular variation by electrophoretic separation of nuclear lens protein was applied for the first time in sharks. 2. 2. The protein was extracted from lens nuclei of 23 sandbar shark pups in a saline-urea solution and electrophoretically separated on cellulose acetate. 3. 3. The protein patterns formed ten types, reflecting genetic heterogeneity. 4. 4. This approach can be used in sharks to study intraspecific genetic variation and to identify separate breeding populations, as in teleosts. 5. 5. Older sharks have a decreased amount of soluble nuclear lens protein, which may be due to ontogenetic factors or denaturation effects of intrinsic urea.

A proposed phylogenetic relationship between sea cucumber Polian vesicles and the vertebrate lymphoreticular system

Abstract Evidence is presented that Polian vesicles of the sea cucumber, Holothuria cinerascens, a member of an echinoderm class considered close to the vertebrate evolutionary line, are organs of inflammatory (including immunologic) responsiveness. As such, they might represent a rudimentary beginning of what later evolved into the vertebrate lymphoreticular system.

An electrophoretic study of protein extracted in distilled water and in saline solution from the eye lens nucleus of the squid, Nototodarus hawaiiensis (Berry)

Abstract 1. 1. Left lens nuclei from fourteen squid, Nototodarus hawaiiensis , were separately extracted in distilled water; right lens nuclei were extracted in 0.14 g% saline solution. 2. 2. Electrophoretic separation of the proteins extracted in each medium produced six different patterns of five to eleven fractions, with most patterns having six bands. Anodally migrating protein extracted in distilled water produced the most distinctive pattern variations. 3. 3. The method of electrophoretic separation of nuclear lens protein is applicable to identifying separate breeding populations of squid. 4. 4. Nuclear lens protein of squid and of vertebrates is alike in solubility characteristics, in most migrating toward the cathode and in varying intra-specifically.

Effects of urea on solubility and electrophoretic characteristics of protein from the eye lens nucleus in bigeye and skipjack tunas, and in menpachi

Abstract 1. 1. A solution of urea was sought which would solubilize the albuminoid present in the eye lens nucleus without degrading the soluble lens proteins or producing undesirable effects in electrophoretic patterns. 2. 2. Tests on extracts of macerated, pooled lens nuclei from bigeye and skipjack tunas, and from menpachi, revealed that the most effective extracting solution for albuminoid is composed of 0·14 g% NaCl, 0·1 M urea, with 3 drops of merthiolate (10 −5 ) (preservative) to make up 50 ml. 3. 3. The solubility characteristics of the nuclear lens proteins reflected the closer relationship between the two tunas than between either tuna and the menpachi.

Digestive gland and integument lesions associated with malnutrition in a ghost shrimp, Callianassa affinis☆

Abstract A ghost shrimp, Callianassa affinis , maintained alone in an aerated seawater aquarium, refused food for 2 months. During this time it developed grossly visible lesions in the integument, became progressively more listless, and finally died. Histologic study of selected tissues revealed an abnormal accumulation of fat and a marked blood-cell response in the digestive gland (“liver”). The integument lesions consisted primarily of fragmented cuticle underlain by blood cells in various stages of necrosis. Blood cells further from the surface were healthier and were frequently seen in whorls of one or more cell layers around pigmented material. A likely cause of death was digestive gland failure due to a lack of dietary lipotropic factors that, in mammals at least, normally prevent excessive fat accumulation in the liver. The integument lesions may represent pathological changes that are part of a syndrome of malnutrition.

Tumefactions (tumorlike swellings) on the foot of the moon snail Polinices lewisii

Abstract The moon snail Polinices lewisii, with several large masses on the foot, was recovered alive from the ocean bottom. Although the lesions outwardly resembled neoplastic growths, microscopic examination revealed mainly scattered muscle fibers and edematous fluid. This fluid contained numerous and diverse microorganisms which also were present in large numbers in the surrounding “normal” tissue and in most internal organs. An amoebocytic response was not apparent. These tumefactions (tumorlike swellings) apparently developed in response to a widespread infection and represent foci of edema, rather than neoplasms.