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Biomedical subjects

S Sho

Publications and source records attributed to S Sho.

At least 19 recordsLinked to original sources
PubMed1997

Placental cavities.

OBJECTIVE: To study placental cavities by gross and microscopic examination and ultrasonography and their frequency with various epidemiologic factors and intervillous thrombosis. METHODS: After formalin fixation, interval sections of 567 placentas were prepared to search for cavities and intervillous thrombosis. Cavities were subjected to histologic and ultrasonographic examinations. RESULTS: Frequency of cavities with diameter of 1 cm or more was 34.9% in 567 mature placentas. Frequency of cavities was significantly higher in heavy, thick placentas associated with male fetuses. Histologic examination revealed villus laceration in cavities and syncytial cells, isolated chorionic villi, or air bubbles in placental fetal veins. All 82 placentas with cavities showed villus lacerations in the cavities and air bubbles in the fetal veins. Intervillous thromboses in fetal lobules were located only in the cavities. Cavities were first found by ultrasonography at a mean gestational age of 30.9 +/- 3.8 weeks. Ultrasonography did not always differentiate accurately between intervillous thrombosis and cavities. CONCLUSION: Placental cavities were found significantly more often in heavy, thick placentas associated with male fetuses. Strong uterine contractions during placental detachment could produce villus laceration in cavities, following contamination by air bubbles and isolated villus tissue in the fetal veins. Placental cavities are vulnerable to villus laceration. Intervillous thrombosis occurred only in cavities.

Female↗
PubMed1990

Isoelectric analysis of 3H-pargyline-labelled monoamine oxidase in rat and carp.

1. After selective binding of [3H]pargyline to either monoamine oxidase (MAO) A or MAO B in the rat liver, MAO B alone in the rat brain and MAO in carp brain and liver, molecular weight and isoelectric points (pI) of these MAO were determined by sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis and isoelectric focusing and results obtained were compared. 2. For all tissues tested, SDS-polyacrylamide gel electrophoresis of [3H]pargyline-bound samples revealed a labelled protein band of an apparent mol. wt of 60,000 da. 3. Estimation of radioactivity of [3H]pargyline bound after isoelectric focusing revealed a single protein band with acidic pI values of about 5.5 for rat brain and liver MAO B. 4. Moreover, the pI values of about 7.5 were obtained for carp brain and liver MAO. This basic value was also found for MAO A in the rat liver MAO A.

Animals↗
PubMed1989

Spectrophotometric kinetic studies and substrate inhibition of hog kidney histaminase activity by an improved 2,4-dinitrophenylhydrazine method.

We improved the experimental procedure for the measurement of hog kidney histaminase activity using histamine as a substrate on the basis of a spectrophotometric estimation of the 2,4-dinitrophenylhydrazone of imidazole acetaldehyde and studied the steady-state kinetics to obtain the basic data for further investigations of the oxidative deamination of histamine. The initial and mean velocities of the enzymatic reaction were calculated and plotted against the amount of enzyme. It was found that the initial velocity increased linearly. The time t alpha necessary to reach the extent of reaction alpha was calculated and plotted against the reciprocal of the enzyme concentration eO. It was found that t alpha was linearly proportional to 1/eO. From Lineweaver-Burk plots, inhibition by high concentration of substrate was evident, and the v-pS curve was bell-shaped, with a pS maximum at 3.2. Km and V were obtained: Km = 7.7 x 10(-5) M, V = 0.0026 mumol/min (0.00075 mumol/min/mg protein). It was concluded that our DNP method was useful for the measurement of hog kidney histaminase activity using histamine as a substrate, basic steady-state kinetic studies and further investigations of substrate inhibition and inhibitory effect.

Amine Oxidase (Copper-Containing)↗
PubMed1985

[Molecular weight of mitochondrial type B MAO in various organs of guinea pig].

Molecular weights of mitochondrial type B monoamine oxidase (MAO) in guinea pig brain, liver and kidney were estimated, and their identities and multiplicity were studied. We ascertained what concentration of 3H-pargyline bound to type B MAO specifically from the inhibition curve toward serotonin (5-HT) and beta-phenylethylamine (beta-PEA) by pargyline. Pargyline irreversibly binds to FAD in MAO at a one to one molecular ratio. 3H-pargyline bound to type B MAO specifically and irreversibly by incubation for 5 hr at 37 degrees C, and SDS-disc electrophoresis was carried out using 3H-pargyline as a tracer. The molecular weight of MAO was estimated after specific binding of pargyline was corrected for non-specific binding. The molecular weight of type B MAO in every organ was found to be 60,000, giving a single peak after solubilization with 6% SDS, but several peaks at higher molecular weight were found in each organ after solubilization with 2% SDS. In the brain, there appeared to be a peak of 100,000, and it was suggested that the MAO existed as a dimer which was composed of a FAD containing subunit and a low molecular weight subunit containing no FAD. In the liver, there appeared to be peaks of 120,000 and 240,000, and it was suggested that the MAO existed as a dimer and tetramer. In the kidney, there appeared to be a peak of 180,000, and MAO was suggested to exist as a trimer.

Animals↗
PubMed1984

Enzymic and molecular characteristics of a new form of monoamine oxidase, distinct from form-A and form-B.

The present study was undertaken to clarify the enzymic and molecular properties of monoamine oxidase (MAO) in carp brain. In particular, its sensitivities to selective MAO inhibitors, kinetic properties and molecular weight were compared with those of the enzyme in carp liver. The selective and potent MAO-A and MAO-B inhibitors FLA 788(+), FLA 336(+), MD 780236 and benzylcyanide caused dose-dependent inhibitions of MAO activity in both carp brain and liver; the inhibition curves were all single-sigmoidal, and the degrees of inhibition of the activities towards 5-hydroxytryptamine (5-HT, selective MAO-A substrate), tyramine (substrate for both forms of MAO) and beta-phenylethylamine (PEA, selective MAO-B substrate) were similar. This was also the case for inhibition of activity in carp brain by the irreversible and selective MAO-A and MAO-B inhibitors clorgyline and I-deprenyl, indicating the presence in both preparations of a single MAO which differs from either form of MAO. Studies on the substrate specificities and Km values for these three substrates and the inhibitory effects of some compounds suggested that the enzymic characters of MAO in carp preparations were similar and that these enzymes might be FAD-containing enzymes, like MAO in various mammals. By labelling the preparations with radioactive pargyline and then subjecting them to sodium dodecyl sulfate electrophoresis, the apparent molecular weights of carp brain and liver MAO were estimated as 60,000 daltons. The same value was also obtained for rat brain and liver mitochondrial MAO-B. These results indicate that by the present definitions of MAO-A and MAO-B, MAO in carp brain and liver is similar to, but distinct from, both these forms of MAO.

Animals↗
PubMedDate not supplied

Effect of physiological fluids on radical intensity of sodium ascorbate and sodium 5,6-benzylidene-L-ascorbate.

The effect of various physiological fluids on the radical intensity of sodium ascorbate and sodium 5,6-benzylidene-L-ascorbate (SBA) was investigated using ESR spectroscopy. Blood from various animals did not significantly affect the radical intensity of both ascorbates, whereas the corresponding plasma fractions significantly enhanced the radical intensity. This suggests that some populations of blood cells might modify the interaction between plasma components and ascorbates. Saliva contained labile substance(s) which effectively reduced the ascorbate radical intensity. HPLC demonstrated the presence of endogenous ascorbate in rat liver and brain homogenates. When sodium ascorbate or SBA was incubated with any of these homogenates, their radical intensity was synergistically enhanced, but abruptly declined without any apparent ascorbate degradation. Incubation with homogenates elevated the radical intensity of SBA up to the level significantly higher than that of sodium ascorbate. The present data suggest that antitumor action of SBA might be mediated via the accelerated production of ascorbate radical in the target organ.

Animals↗