Fumio Matsuura

Linkages between chromophore and apoprotein in the biliverdin-protein of the scales of big blue parrotfish, Scarus gibbus Rüppell

On the basis of the amino acid composition of the chromophore peptides, it can be assumed that Asp, Ser and 1/2 Cys are located near the biliverdin chromophore. Experiments for splitting of the chromophore lead us to expect a thioether bond in the linkages between biliverdin and apoprotein.

Identity of blue pigments obtained from different tissues of the sculpin, Pseudoblennius percoides Günther

Abstract 1. 1. Blue chromoproteins were isolated from the skin, muscle, digestive tract and eggs of the sculpin, Pseudoblennius percoides Gunther. 2. 2. They showed the same absorption spectrum and almost the identical molecular weights (38,000–42,000) and isoelectric points (3.4–3.7). 3. 3. The identity of these chromoproteins was confirmed by isoelectric focussing with mixed samples. 4. 4. Their chromophores were identified as being solely biliverdin IX 2 . 5. 5. It may be concluded that one and the same biliverdin-protein exists in the different tissues of this fish.

Advanced optimization of permanent magnet wigglers using genetic algorithm

In permanent magnet wigglers, magnetic imperfection of each magnet piece causes field error. This field error can be reduced or compensated by sorting magnet pieces in proper order. We showed a genetic algorithm has good property for this sorting scheme. In this paper, this optimization scheme is applied to the case of permanent magnets which have errors in the direction of field. The result shows the genetic algorithm is superior to other algorithms.

Studies on myosin of spiny lobster -I isolation and physico-chemical properties.

A method for preparation of purified myosin from the abdominal muscle of spiny lobster was devised and the physico-chemical properties of the myosin obtained were examined. Intrinsic viscosity, sedimentation constant (s020, w), and diffusion constant (D020, w) of the myosin were 2.05dl/g, 6.65S, and 1.35×10-7cm2sec-1, respectively. The molecular weight was determined to be 445, 000±15, 000 (MS, D) and 500, 000±50, 000(Me). The myosin was precipitated with ammonium sulfate between 40 and 50% saturation at pH 7.0, and salted in with more than 0.15M KCl at pH6.5. The above physico-chemical properties as well as amino acid composition of spiny lobster myosin resemble, as a whole, those of other myosins so far reported.

Studies on a green pigment in the erythrocytes of skipjack. III. Sugar, base, phosphate, and lipid moieties.

The three major components (I, II, and VI) of the green pigment from skipjack erythrocytes were analyzed for sugar, base, phosphate, and lipid moieties. The sugar moiety was mainly ribose, and its content ranged from 12 to 17% depending upon the component. The base moiety was composed of adenine, guanine, cytosine, and uracil, the total content being 3-4% in all three components. The phosphate content ranged from 6% (component VI) to 18%. (component II). The lipid content of component II, the only component analyzed for lipid, was 15% and consisted of glyceride, free fatty acid, and phospholipid.

N-Terminal Amino Acid of Eel Hemoglobin

The 4 Hb components of eel were isolated and analyzed for N-terminal structure. Only 2 N-terminal valyl residues per molecule were detected by the DNP method for each component. On the other hand, the presence of 2 acetyl groups per mole-cule was demonstrated in all the components by paper and gas chromatography and by the colorimetry of ferric-hydroxamic acid complex derived. Based on those results, it may be concluded that each of the 4 Hbs has 2 valyl and 2 N-acetylated amino acids as N-termini.

CHEMICAL STUDIES ON THE RED MUSCLE (“CHIAI”) OF FISHES-XIII

Alkali denaturation curves of hemoglobin (Hb) and myoglobin (Mb) of fishes were determined mainly in oxy form under various conditions. The results obtained were as follows. Denaturation curves of oxy-Hb of the fishes except flathead appeared between those of horse (fairly resistible Hb among mammalian Hbs2, 10)) and human Hb (least resistible Hb2, 10)) (Fig. 7). Therefore, there seems to be no clear inter-specific specificity of Hb between fishes and mammals in the alkali resistibility. Specificity may be pointed out, however, on the shape of the denaturation curve; the curves of mammalian Hbs were almost straight, indicating that the denaturation was of the first order reaction, whereas those of fish Hbs were not. The alkali denaturation curves of fish Hbs were different considerably from one another, both in the slope and in the shape of them. Thus the alkali resistibility may be regarded as one of the representations of intra specific specificities of fish Hb. Though Hbs of many fishes showed gently curved lines, those of some fishes such as carp, mullet, big-eye tuna, and chum salmon presented sharply bended lines, just as suggesting that they are consisting of two components different in alkali resistibility. Hbs of carp and mullet are, however, electrophoretically homogeneous6). Although two Hbs were seen also on electrophoresis in the case of chum6), the proportion of both components as estimated from its denaturation curve was not agreeable with that calculated from the electrophoretic pattern. In addition, as seen in the case of carp (Fig. 6), the shape of the denaturation curve was markedly different at various pHs. Because of these facts, the alkali denaturation method may be not so useful to analysis of multiple Hbs of fish. Met-Mb of tuna was much more resistant to alkali denaturation than met-Hb of the same fish (Fig. 10). In order to investigate whether the difference in alkali resistance between both pigments of tuna is applicable to the simultaneous determination of them as previously described in the case of human7), experimental conditions (such as derived form of pigments, pH, and time of reaction) under which Mb remains native and Hb denatures completely, were looked for in vain (Figs. 9 and 11, Table 1).

Chemical Studies on the Red Muscle (“Chiai”) of Fishes-VIII

Crystalline cytochrome c (Cyt) was prepared from the red muscle of tuna, Neothunnus macropterus, by the method of HAGIHARA4, 9) with some modification (Fig. 1). The twicerecrystallized preparation was then analyzed for the iron content, spectral and electrophoretic properties. The iron content of this preparation was found to be 0.487%, which is slightly higher than the values of crystalline Cyts from other sources (0.43-0.47%)2, 3, 6). The spectral characters agreed fairly well with those for amorphous Cyts reported before1), except the lower absorption coefficient for minimum (about 535mμ), which makes the ratios of e550/e535 and e520/e535 higher (Fig. 2 and Tables 1 and 2). The electrophoretic experiments revealed the general resemblance of pH-mobility curve of tuna Cyt to those of horse, beef, pig, and chicken18), though Cyt of the former moved more rapidly than the latter in the strongly acidic or alkaline pH range (Fig. 3). The isoelectric point of tuna Cyt was found to be pH 10.2, which is slightly lower in pH value, as compared with those of all the other species above-mentioned (pH 10.7-10.9)18).