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Biomedical subjects

M Endo

Publications and source records attributed to M Endo.

At least 1,081 records · Page 60Linked to original sources
PubMed1980

[Experiences on stereotaxic hypophysectomy for recurrent breast carcinoma; with particular reference to its pain relief (author's transl)].

Stereotaxic hypophysectomy was performed in nine patients with advanced breast carcinoma. Only one patient showed an objective remission in the form of decreased size of the chest wall ulcer after the operation. However, all but one patient did get relief of pain lasting for months. In one of these cases, where hypophyseal ablation was carried out under local anesthesia, pain relief was ascertained immediately after the ablation, i.e., during the operation. Such an instantaneous pain relief, which to the author's knowledge has never been described elsewhere, was considered to be the result of an influence on the hypothalamus rather than the pituitary itself. Mechanism of lasting pain relief was ascribed to endorphins which have recently attracted attention as endogenous peptides with opiate-like activities. Pituitary ablation of the present authors were noted to be incomplete either seen from hormonal assessment or from morphological evaluation. It was stressed that significant pain relief could be gained by the apparently incomplete hypophyseal ablation, whereas complete destruction does not necessarily guarantee a hundred percent relief of pain. A deduction was made that although endorphins may play an important role in alleviating pain, integrity of its productive system and/or its receptors could also be important as well. Stereotaxic hypophyseal ablation might be the procedure of choice in certain patients with advanced breast carcinoma suffering from excruciating pain.

Breast Neoplasms↗
PubMed1979

Isolation and characterization of L-fucose dehydrogenase from rabbit liver.

L-Fucose dehydrogenase [EC 1.1.1.122] was isolated from a rabbit liver extract and purified about 390-fold with a yield of approximately 13%. The purification procedures included treatment with protamine, ammonium sulfate fractionation, treatment with acid, DE-32 celluose colum chromatography, gel filtration on Sephadex G-100, preparative polyacrylamide gel electrophoresis, and affinity chromatography on 5' AMP-Sepharose 4B. The last procedure, affinity chromatography on 5' AMP-Sephadex 4B, was useful for the removal of other dehydrogenases. The eznyme which was homogeneous, as shown by polyacrylamide gel electrophoresis, had a molecular weight of about 92,000. The optimum pH was at 10.0 and isoelectric point at 5.2. The enzyme accepted both L-fucose and D-arabinose as substrate, but was specific for NAD+ as coenzyme. Km values were 0.15 mM, 1.4 mM, and 0.7 mM for L-fucose, D-arabinose, and NAD+, respectively. A single enzyme catalyzed the oxidation of L-fucose and D-arabinose, which had the same configurations of hydroxyl groups from C-2 to C-4. The reaction products obtained with L-fucose as substrate were L-fucono-lactone and L-fuconic acid. The L-fucono-lactone was an immediate product of oxidation and was hydrolyzed to L-fuconic acid spontaneously. This reaction was irreversible. Therefore, it is likely that L-fucose dehydrogenase is involved in the initial step of the catabolic pathway of L-fucose in rabbit liver.

Animals↗
PubMed1979

Glucose-containing oligosaccharides in normal human urine.

Normal human urine was treated with cetylpyridinium chloride (CPC), and the CPC-supernatant was passed through columns of Dowex 50 X 2 (H+ form) and Dowex 1 X 2(Cl-form) in succession. The concentrated effluent containing neutral saccharides was then gel-filtered through a column of Sephadex G-10. The resulting effluent was divided into 5 subfractions (SFs. 1-5). Comparison of hexose contents of the subfractions indicated that healthy individuals regularly excreted neutral oligosaccharides in urine with a similar pattern regardless of age or sex. Component A isolated from SF2 was characterized as glucosylgalactose by paper chromatography before and after acid hydrolysis of the intact one and its reduction product.

Adolescent↗
PubMed1979

Isolation and characterization of proteohyaluronic acid from human umbilical cord.

Proteohyaluronic acid was extracted from human umbilical cord with 0.2% NaCl, then purified by cetylpyridinium chloride(CPC)-precipitation, DEAE-cellulose column chromatography, gel-filtration on Sephadex G-200 and on Sepharose 4B, in succession. The purified preparation contained glucosamine (40.1%), glucuronic acid (45.7%) and protein (2.6%). Glutamic acid, glycine, alanine, serine and aspartic acid were the major amino acids of the protein moiety. The result of the gel-filtration suggested that an average molecular weight was more than 1 x 10(6). Although analytical data for the constituent sugars and infrared spectra were similar before and after pronase digestion of this proteohyaluronic acid, the mobilities in electrophoresis and the elution patterns of gel-filtration differed remarkably from one another. Since the protein content decreased from 2.6% to 0.3% by the proteolytic digestion, it is evident that the degraded protein moiety played an important role in maintaining the macromolecular structure of this proteohyaluronic acid.

Amino Acids↗
PubMed1979

A method for micro-scale isolation of sulfated glycopeptide from tissue.

Micro-scale isolation of sulfated glycopeptide from tissue was achieved by successive application of pronase digestion (Step 1), cetylpyridinium chloride-fractionation (Step 2), crude heparinase digestion or chondroitinase ABC digestion plus nitrous acid treatment (Step 3) and preparative cellulose acetate membrane-electrophoresis (Step 4). By this method, sulfated glycopeptide was obtained in a high yield from estrogen-treated rabbit uterus.

Animals↗