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Biomedical subjects

K Shibasaki

Publications and source records attributed to K Shibasaki.

7 recordsLinked to original sources
PubMed1979

Spinal osteotomy to correct kyphosis in spinal tuberculosis.

Twenty-seven patients with severe tuberculous kyphosis have been treated at the National Murayama Hospital between 1966 and 1977. We have undertaken curettage of the foci and vertebral osteotomy through an anterior approach, followed by gradual correction with a halo pelvic distraction apparatus and subsequent vertebral fusion. Choice of this method depends upon the age of the patient, the degree of kyphosis before correction, and the presence of concomitant lesions. Details of postoperative management are given and their importance is emphasized. The major risks of correction are discussed and precautions suggested.

Adolescent↗
PubMed1978

Changes of LH, TSH, GH, FSH and PRL in pituitaries and sera of rats after thyroidectomy and thyroxine treatment as studied by radioimmunoassay and disc electrophoresis.

Rat pituitary hormones (LH, TSH, GH, FSH and PRL) were located in polyacrylamide gels after the separation of rat pituitary homogenate with the aid of electrophoresis. Furthermore, the incorporation of 3H-glucosamine and 14C-leucine into various protein fractions of incubation media and pituitaries incubated for 6 h in vitro, homogenized and then subjected to disc electrophoresis was measured in six groups of rats: 1. control; 2. two weeks after thyroidectomy (Tx); 3.--6. two weeks after thyroidectomy and injected 20 micrograms L-thyroxine (T4) i.p. per animal at 6, 12, 24 and 48 h before sacrifice, respectively. A decrease of 14C-leucine incorporation into GH and PRL after thyroidectomy was found which was improved by T4 treatment. Moreover, an increase of 3H-glucosamine and 14C-leucine incorporation into TSH zone and origin zone was observed, the former presumably representing the extracted TSH and the latter consisting of unextracted portion of TSH, other hormones and unidentified proteins. Such increase was significantly less after T4 treatment. Finally, changes of radioimmunoassayable LH, TSH, GH, FSH and PRL in pituitaries and sera of analogous groups of rats, but consisting of another animals were measured. The content of TSH in the pituitary slightly increased after Tx, but increased further after T4 treatment. In contrast, the content of all other hormones in the pituitary decreased after Tx, while T4 treatment resulted in a stepwise increase. In plasma, a significant decrease of GH and PRL after Tx was found with no remarkable changes after T4 treatment. The level of LH and FSH was unchanged, while that of TSH increased significantly after Tx and sharply decreased to the original level as early as at 6 h after the injection of T4.

Animals↗
PubMed1978

Vertebral metastases and spinal cord compression.

Clinical interest in spinal compression and resultant paraplegia due to metastases has mounted in recent years. This has stimulated attention to the neuropathology of the condition. 14 cases of spinal cord compression due to vertebral metastases are compared with over 100 traumatic cases. In the traumatic lesions there is central haemorrhagic necrosis leading to cavitation and gliosis with nerve root regeneration in the late stages. In the metastatic cases, lesions are often peripheral, pie-shaped and are related to vascular factors. The neuropathology of cord necrosis due to metastatic spinal disease is therefore different from that caused by trauma. These observations have clinical importance in planning treatment.

Adult↗
PubMed1977

Beta-conglycinin from soybean proteins. Isolation and immunological and physicochemical properties of the monomeric forms.

Beta-conglycinin consisting of six major isomers (designated B1- to B6-conglycinin) was dissociated and fractionated on columns of DEAE- and CM-Sephadex in buffers containing 6 M urea. Three major (alpha, alpha' and beta) and one minor (gamma) subunits were isolated and further characterized by gel electrophoresis and gel electrofocusing. Gel electrophoresis in urea and in sodium dodecyl sulfate, and gel filtration in 6 M guanidine hydrochloride gave a molecular weight of 57 000 for alpha, alpha' subunits; and 42 000 for beta and gamma subunits. The isoelectric points of the isolated subunits, measured by disc gel electrofocusing, were as follows: alpha, 4.90; alpha', 5.18; beta, 5.66-6.00. On gel electrofocusing, beta subunit showed four microheterogeneous components; three of them comprised 95% of the total beta subunit. Leucine and valine were the N-terminal amino acids of beta and alpha alpha' subunits, respectively. The isolated subunits contained mannose and glucosamine in varying quantities. Two carbohydrate moieties were calculated for one mole of alpha, alpha' subunits; and one carbohydrate moiety for the beta subunit. Considerable similarity in the amino acid composition of alpha and alpha' subunits was observed. The beta subunit was devoid of cysteine and methionine; and in comparison with alpha, alpha' subunits, had a higher content of hydrophobic amino acids. The isolated subunits exhibited antigen-antibody reaction with antisera to the native beta-conglycinin. Each of them was partglycinins. The alpha and alpha' subunits were in addition identical with each other and with B5-, B6-conglycinins. They were immunologically unrelated with beta subunit. The recovery of immuno-properties from the individual subunits may be attributed to the reconstruction of the three-dimensional structure upon removal of denaturing reagents.

Amino Acids↗
PubMed1976

Heterogeneity of beta-conglycinin.

Beta-conglycinin, a major 7 S soybean globulin, purified by ion-exchange and gel chromatography was fractionated into six distinct components on columns of DEAE-Sephadex. The six components (designated B1 to B6-conglycinins) were characterized by disc electrophoresis. Gel electrophoresis and gel electrofocusing in dissociating buffers indicate that the six conglycinins are isomers containing varying proportions of three kinds of subunits (alpha, alpha' and beta). The subunit structures of these isomers are alpha' beta (B1-), alpha beta (B2-), alpha alpha' beta (B3-), alpha beta (B4-), alpha alpha' (B5-), and alpha (B6-conglycinin). Beta subunit is a major constitutent of B1- and B2-conglycinins, whereas B3- to B6-conglycinins are composed predominantly of alpha subunit. The six beta-conglycinins are all glycoproteins containing mannose and glucosamine. They differ in the N-terminal amino acid composition. The isolated B1- to B4-conglycinins are immunologically identical with one another and with the total beta-conglycinin. B5- and Bl-conglycinins which comprise no beta subunit are partially identical with the total protein. Some antigenic determinants that are lacking in the B5- and B6-conglycinins are expected to be located on the beta subunit.

Amino Acid Sequence↗