Biomedical subjects
Publications and source records attributed to K Ohashi.
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beta-Actinin, a minor regulatory protein of muscle, was purified from skeletal muscles of rabbit and chicken by DEAE-Sephadex chromatography. beta-Actinin consisted of two subunits, beta I and betaII, with chain weights of 37,000 and 34,000 daltons, respectively. The amino acid compositions were similar, though not identical. It appears that each of the two subunits is associated in solution. beta-Actinin had the following effects on actin: (1) inhibition of reassociation of F-actin fragments; (2) inhibition of network formation of F-actin; (3) inhibition of growth of F-actin fragments; (4) retardation of depolymerization of F-actin and (5) acceleration of polymerization of G-actin. All these actions of beta-actinin can be explained in terms of action as an "ending factor". Experimental evidence favored the view that beta-actinin is bound to one end of the F-actin filament, namely to the end opposite to the direction of polymerization. Fluorescence-labeled anti-beta-actinin stained the middle portion of the A band of myofibrils. Based on the finding that the stain was unchanged on removal of myosin, it is suggested that beta-actinin is located at the free ends of the I filaments of myofibrils. Thus is seems likely that beta-actinin functions as an ending factor for actin filaments.
A new minor regulatory protein designated as I-protein has been isolated from skeletal muscles of the chicken and the rabbit. The yield of purified I-protein was small: 5-10 mg per kg of muscle. I-protein was found to have a molecular weight of 50,000 and high contents of Asp and Glu, accounting for more than one third of the total amino acids.
Rabbit antiserum raised agains I-protein was used for immunofluorescent staining of chicken myofibrils. The FITC-conjugated anti-I-protein antibody stained A-band regions except at their middle regions. According to the conditions used, the myofibrils stained by their fluorescent antibody showed slightly different patterns, i.e., the nonstained regions in the center of the A-bands were wider. On fixing with glutaraldehyde, myofibrils were stained in the A-band regions except at their middle regions. Therefore, I-protein may be localized at A-bands except for the center.
I-protein inhibited theMg-activated ATPase [EC 3.6.1.3] activity of actinomyosin by approximately 50% at low ionic strength. Concomitantly, the onset of superprecipitation was retarded. I-protein was found to bind to myosin, but not to F-actin. The inhibitory action of I-protein occurred only in the absence of Ca ions in the troponintropomyosin-actin myosin system. Addition of Ca ions abolished the effect. Thus, it is very likely that I-protein prevents unnecessary hydrolysis of ATP in the relaxed state of muscle.
On agarose gel electrophoresis the pancreatic serum isoamylases can be separated into a main fraction and more anodally migrating minor fractions. In acute pancreatic hyperamylasemia as in normal subjects the activity of the anodally migrating pancreatic amylase does not exceed 20% of the activity of the main fraction. In patients with pancreatic main duct occlusion or stenosis with or without calculi or cysts, the anodally migrating pancreatic amylase increases proportionally more than does the main fraction, and can even be stronger than the main fraction. The majority of these patients also had abnormally increased total pancreatic serum amylase activity.
Connectin, an elastic protein, was isolated from both skeletal and cardiac muscles of various species of vertebrates, and also from smooth muscles (gizzard) of the chicken. The amino acid compositions of these preparations were very similar. Connectin was also obtained from claw and tail muscles of the crayfish, but preparations from clam adductor muscles and insect thoracic muscles were heavily contaminated with collagen and resilin, respectively. Connectin-like protein was obtained from cell membranes of erythrocytes and fluorescent anti-connectin staining suggested that it is located on the cytoplasmic surface of the membrane. An attempt to isolate an elastic protein from insoluble residues of amoebae of the slime mold and those of bacterial cell body (Salmonella) was inconclusive. The present comparative bio-chemical study has shown that connectin or connectin-like protein is widely distributed in various types of muscles and in some nonmuscle cells.
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An elastic protein was isolated from the cortical layer of the fertilized eggs of two species of sea-urchin. Young's modulus of the fiber of the sea-urchin protein was approximately 1-10(7) dyne/cm2. The amino acid compositions of the elastic protein from the two species of sea-urchin eggs were very similar to that of connectin, elastic protein from vertebrate skeletal muscle. The fluorescent antibody against muscle connectin stained the cortical layer of the sea-urchin egg. It appears that the elastic protein is responsible for the elasticity of the egg cortex.
The nucleotide seuquence of Escherichia coli asparagine tRNA was determined to be pU-C-C-U-C-U-G-s4U-A-G-U-U-C-A-G-D-C-G-G-D-A-G-A-A-C-G-G-C-G-G-A-C-U-Q-U-U-t6A-A-phi-C-C-G-U-A-U-m G-U-C-A-C-U-G-G-T-phi-C-G-A-G-U-C-C-A-G-U-C-A-G-A-G-G-A-G-C-C-AOH. Its D-stem and D-loop have almost the same sequence as Escherichia coli aspartate tRNA.
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Adult male albino rats of three strains--Wistar, Sprague-Dawley and Holtzman--were trained to press a lever to avoid electric shocks under Sidman-type (R-S interval-20 sec; S-S interval=5 sec) and discriminated avoidance (ITI-15 sec; warning duration=5 sec) schedules, and the acquisition processes of avoidance responses, and the properties of behavioral baselines were investigated. Under both schedules, Wistar strain rats, though showing poorer results than the other two in the beginning, rapidly progressed with the repetitive training, and finally displayed excellent and stable performances. Srague-Dawley strain rats were poorer in performances, with delayed acquisition and prolonged warm-up effect in the within-session performance. The results of Holtzman strain rats ranked between the two. After the establishment of stable behavioral baselines under both schedules, 0.5, 1.0 and 2.0 mg/kg of diazepam were given subcutaneously, and it was found that in Wistar and Holtzman strain rats, the avoidance responses were inhibited together with increase of delivered shocks in parallel to the doses. In Sprague-Dawley strain rats, however, the avoidance responses were conversely improved with 0.5 and 1.0 mg/kg, while such tended to be inhibited with 2.0 mg/kg, with marked concomitant ataxia. As definite strain differences in avoidance response were demonstrated herein, selection of the most appropriate strain should be made when designing behavioral experiments.
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