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Biomedical subjects

K Ogata

Publications and source records attributed to K Ogata.

At least 523 records · Page 29Linked to original sources
PubMed1979

Studies on the protein components of 110S and total ribonucleoprotein particles of rat liver nucleoli.

Proteins of rat liver nucleolar RNP, especially 110S RNP containing 45S RNA, were investigated and the following results were obtained. 1. Nucleolar extract was prepared from thioacetamide-treated rat liver nucleoli in the presence of 1 mg PVS per ml. Sucrose-density gradient centrifugation of the nucleolar extract showed RNP distributed between 60S and 110S. The 110S particles (110S RNP) contain 45S RNA as judged from the radioactivity profiles of nucleolar extract labelled in vivo with [3H]orotic acid for 10 min and 2 h. The protein components of 110S RNP and total RNP heavier than 60S (total RNP) were analyzed and compared. 2. Since the effects of PVS treatment on the extraction and the electrophoretic pattern of ribosomal proteins were removed by increasing the Mg2+ concentration during acetic acid extraction, as described in our preceding paper (1), proteins of 110S RNP as well as total RNP from PVS-pretreated nucleoli were extracted with 67% acetic acid containing 334 mM Mg2+ and analyzed by two-dimensional acrylamide gel electrophoresis. Ribosomal proteins masked by contaminating histone spots on the gel were identified by SDS-acrylamide gel electrophoresis. 3. 110S RNP contained a large portion of ribosomal proteins from large subunits; 24 protein spots were distinct, 6 protein spots were faint and 5 proteins (L3, L8, L30, L35, and L36) were missing completely. On the other hand, 110S RNP contained a small number of small subunit proteins; only 6 proteins showed distinct spots, 7 proteins showed faint spots and 12 protein spots were missing. 110S particles contained 11 non-ribosomal proteins, although it is difficult to rule out the possibility that some of them were contaminating chromatin proteins. 4. Total RNP showed electrophoretic patterns of 60S ribosomal proteins similar to those of 110S RNP, although L3 protein was present as a faint spot and 26 proteins showed distinct spots. Total RNP contained more small subunit proteins than 110S RNP; 7 proteins spots were distinct, 10 protein spots were faint and 8 protein spots were missing. The results suggest that some kinds of 40S proteins and L3 protein are attached to 110S RNP during the processing of 110S RNP.

Animals↗
PubMed1979

Proteins of small subunits of rat liver ribosomes that interact with poly(U). II. Cross-links between poly(U) and ribosomal proteins in 40 S subunits induced by UV irradiation.

(1) When rat liver 40 S ribosomal proteins in 6 M urea were were mixed with poly(U) at an appropriate ratio, a precipitate was formed which was also insoluble in the sample solution for two-dimensional acrylamide gel electrophoresis. Analyses by two-dimensional acrylamide gel electrophoresis showed that S7 and S10 proteins (according to our numbering system) had disappeared selectively from the fraction soluble in 6 M urea. These two proteins were present in the fraction insoluble in 6 M urea, and became soluble in the sample solution after treating it with RNase. The results suggest that S7 and S10 proteins have strong affinities for poly(U). When rat liver 40 S subunits were incubated with poly(U), similar results were obtained. (2) After incubation of 40 S subunits with [3H]poly(U) and then with unlabeled poly(U), UV irradiation cross-linked poly(U) to the protein moiety of the 40 S subunit. When the protein fraction insoluble in the sample solution for two-dimensional electrophoresis was prepared from 40 S subunits cross-linked to poly(U) and then subjected to two-dimensional acrylamide gel electrophoresis after RNase treatment, S7 and S10 proteins were detected on the gel. In addition to the S7 protein spot, a triangular area spreading from the spot to the origin contained radioactivity. The results suggest that poly(U) is cross-linked to S7 protein and oligo(U) fragments bound to S7 protein affect its electrophoretic mobility. (3) Ribosomal proteins were prepared from 40 S subunits cross-linked to carrier-free [3H]poly(U) and analyzed by three-dimensional acrylamide gel electrophoresis (Terao, K. & Ogata, K. (1975) Biochim. Biophys. Acta 402, 214--229) after RNase treatment. It was found that S7, S6, and S15 proteins are cross-linked to poly(U). From the results of the present and preceding experiments it is concluded that S7 is the poly(U)-binding protein. The possibility that other proteins in 40 S ribosomal subunits interact with poly(U) is discussed.

Animals↗
PubMed1979

Acute effect of open joint wounds on articular cartilage and synovium in rabbits.

Open joint wounds were made in immature and mature rabbit knees by surgical arthrotomy. The wounds of the right knees were packed open for 5 days and the left knee wounds were closed primarily. The biochemical studies were selected to determine the effect of our treatment regimen on changes in the metabolism of articular cartilage and synovium. Neither closed nor open treatment produced significant changes in enzyme activities measured in the articular cartilage as compared to the controls in either immature or mature rabbits. Most of the synovial enzymes were elevated in the injured joints. There were, however, no significant differences in enzyme activity between the joints treated by either open or closed methods. Our findings suggest that short-term open treatment wounds does not cause matrix degradation in the cartilage nor affect the synovium more than simple arthrotomy.

Acetylgalactosamine↗
PubMed1979

[The range of joint motions of the extremities in healthy Japanese people--the difference according to the age (author's transl)].

The passive range of motion was measured in the shoulder, elbow, forearm, wrist, hip, knee and ankle joints in 624 healthy Japanese persons ranging from the neonatal to 80 years of age, by the method formally decided by the Japanese Orthopaedic Association and the Japanese Association of Rehabilitation Medicine in 1974, followed by a statistical analysis. 1. The joint motions, the range of motion value of which being remarkably different by age, were found among the movements in external rotation and horizontal abduction of the shoulder, extension, abduction, adduction, external rotation, internal rotation of the hip and dorsiflexion of the ankle. 2. Elbow flexion, forearm pronation and supination, wrist dorsiflexion and knee flexion showed little change by age. 3. Extension, external rotation and horizontal abduction of the shoulder, dorsiflexion of the wrist, flexion of the hip, flexion of the knee and dorsiflexion and plantar flexion of the ankle gave values exceeding the normal range indicated by the associations. 4. The fluctuation in the range of joint motion was especially wide in the infant and the aged person.

Adolescent↗
PubMed1979

A simple biplanar method of measuring femoral anteversion and neck-shaft angle.

A simple biplanar roentgenographic technique for measurement of femoral anteversion and neck-shaft angle is described in which no special equipment is required. An anteroposterior roentgenogram of the pelvis and the femoral neck is made with the hip in neutral rotation. The true lateral roentgenogram is made with the patient's limb in a lateral position with the hip and knee flexed and with the entire lateral aspect of the leg in contact with the top of the table. Projected cervicofemoral angulations are measured on the roentgenograms. The method is described to determine the true angles by dynamically illustrating the projected angles. Graphs have been prepared with which one can readily determine the anteversion and neck-shaft angles once the projected cervicofemoral angulations have been measured.

Femur↗