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F Yamada

Publications and source records attributed to F Yamada.

At least 109 records · Page 6Linked to original sources
PubMed1981

Self expression.

Explore the source record for details and available documents.

Communication↗
PubMed1980

Distribution of eyeblink amplitude recorded by an electrode hookup: re-examination.

The present experiment was run to re-examine the distributional properties of the eyeblink amplitude elicited by a burst of 110-dB white noise, recorded by an electrode hookup as recommended in our previous report (Yamada, Yamasaki, & Miyata, 1979). 103 volunteers, 54 males and 49 females, were tested. Analysis showed that the amplitudes were distributed normally when a logarithmic transformation was performed but not when the raw scores were used. We conclude that the amplitude of the startle eyeblink reflex has a log-normal distribution property.

Acoustic Stimulation↗
PubMed1980

[Clinical experience with cefamandole in the field of obstetrics and gynecology (author's transl)].

Cefamandole, a new antibiotic with various characteristics was applied clinically in the field of obstetrics and gynecology, and following results were obtained. Cefamandole was administered to 8 cases with cystitis, 2 cases with pelvic infection. The organisms isolated were 5 cases of Escherichia coli, 4 cases of Staphylococcus epidermidis and one case of Klebsiella. Bacteria disappeared in all cases after 5-day treatment with cefamandole. No side effects of the drug were noticed throughout all cases. From the above mentioned clinical experience, cefamandole is considered to be a useful drug for clinical application.

Abscess↗
PubMed1978

Significance of pathognomonic features of normal-pressure hydrocephalus on computerized tomography.

In some patients with congenital or acquired hydrocephalus, a low-density area is seen around the lateral ventricle on computerized tomography. Above all, in patients with normal-pressure hydrocephalus following subarachnoid hemorrhage, there appears a specific low-density area which is fan-shaped and irregular and which extends from the bilateral anterior horns to the frontal pole. This disappears or decreases with a VP shunt. Improvement of clinical symptoms is proportional to the degree of disappearance of the low-density area. The essential part of the occurrence of symptoms in patients with normal-pressure hydrocephalus depends upon a low-density area on CT.

Brain Neoplasms↗
PubMed1976

Purification and characterization of a proteinase from pineapple fruit, fruit bromelain FA2.

Fruit bromelain FA2, the main proteinase component of the juice of pineapple fruit, has been purified and characterized. 1. Efficient extraction of this enzyme from the crude material was possible using "Cellulosin AP," a microbial polysaccharidase preparation containing cellulase, hemicellulase, and pectinase. The enzyme was purified mainly by successive applications of anion-exchange chromatography, yielding an apparently homogeneous protein as judged by several physical, chemical, and immunochemical criteria. Properties of FA2 include: molecular weight, 31,000; isoelectric point, pH 4.6; absorbance at 280 nm of a 1% solution at pH 7.0 per cm, 19.2. 2. FA2 gave only alanine phenylthiohydantoin upon amino-terminal group analysis by the Edman procedure. Stepwise degradation yielded the amino-terminal sequence Ala-Val-Pro-Gln-Ser-Ile-Asp-Trp-Arg-Asp-Tyr-Gly-Ala. The amino acid composition of FA2 was not markedly different from that of stem bromelain, except for a much smaller lysine content and a smaller alanine content relative to glycine in FA2. FA2 contained neither amino sugars nor neutral carbohydrates as determined by several methods, so FA2 is not a glycoprotein. 3. By labeling the reactive cysteine residue (CYS) with [14C]iodoacetate, the following partial amino acid sequence has been determined. Asn-Glx-Asn-Pro-Cys-Gly-Ala-CYS.

Amino Acid Sequence↗
PubMed1975

Purification and properties of galactosyltransferase from human colostrum.

The galactosyltransferase (Uridine diphosphate-D-galactose: D-glucose 1-galactosyltransferase EC 2.4.1.22) was purified from human colostrum by chromatography on DEAE-cellulose, cellulose phosphate, sephadex G-100, and hydroxylapatite after removal of caseins by centrifugation. The final preparation showed two forms of protein on polyacrylamide disc gel electrophoresis, and both of them exhibited galactosyltransferase activity. The molecular weights of the two forms of the protein were estimated as 44,000 to 45,000 and 55,000 to 57,000 by polyacrylamide disc gel electrophoresis containing sodium dodecyl sulfate. General properties of galactosyltransferase were investigated.

Chromatography↗