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H Shiokawa

Publications and source records attributed to H Shiokawa.

At least 37 records · Page 2Linked to original sources
PubMed1991

The primary structure of two molecular species of porcine organ-common type acylphosphatase.

Electrophoretically homogeneous preparations of organ-common type acylphosphatase from porcine testis and brain were separated into two molecular species by reversed-phase liquid chromatography. From tryptic peptide map analysis, it was inferred that each of the two testis proteins is the same as the corresponding one of the two brain proteins. The complete primary structures of the two acylphosphatases from testis were then determined. The one molecular species consists of 100 amino acid residues: [sequence; see text] The other consists of 98 amino acid residues identical to the 3rd-100th residues of the above sequence and is also acetylated at the amino-terminal alanine. The 98-residue sequence has only 59% homology with porcine muscle acylphosphatase, but has 92% homology with human erythrocyte acylphosphatase. It was thus confirmed that the major acylphosphatases in testis, brain, and erythrocyte belong to the same organ-common type isoenzyme, distinct from the muscle type isoenzyme.

Acid Anhydride Hydrolases↗
PubMed1991

Effects of tryptophane on SHRSP offspring growth.

The effects of tryptophane on growth and hypertension of offspring obtained from mothers given L-tryptophane prior to mating: In the tryptophane group, body weights were heavier and blood pressures were higher than in the control group. Stroke lesion incidence rates were also much higher in the tryptophane group. At 20 weeks of age, brain enzyme activities were lower and serotonin content was higher in the tryptophane group in comparison with the control. These results suggest that dietary tryptophane may affect precocious maturation and as well as affect elevation in blood pressures due to brain serotonin turnover.

Animals↗
PubMed1991

Therapy and prevention of hypertension of M-SHRSP.

M-SHRSP rats appear to be a useful animal model for studying juvenile human malignant hypertension. Using M-SHRSP, the present study was conducted. Drugs selected for use were captopril, SQ 29,852 and hydralazine hydrochloride. The rats were also fed a 33% fish meal diet. When given separately, all three drugs were shown to be anti-hypertensive. However, using the fish meal diet combined with hydralazine was more effective than were any of the drugs given separately, while the effect of hydralazine combined with captopril or SQ 29,852 was even greater than that of the combined fish meal diet and hydralazine treatment. Some rats treated with captopril or SQ 29,852 separately were resistant to treatment, however even for these rats life spans were significantly prolonged and hypertensive vascular lesion incidence rates were drastically lowered. It was also found that even such vascular lesions as angionecrosis seemed to disappear with captopril or SQ 29,852 treatment.

Angiotensin-Converting Enzyme Inhibitors↗
PubMed1991

Chronic treatment with captopril, SQ29,852, hydralazine and a 33% fish meal diet in malignant stroke-prone spontaneously hypertensive rats.

Malignant stroke-prone spontaneously hypertensive rats (M-SHRSP) are a useful animal model for studying juvenile malignant hypertension. Using M-SHRSP males, the effects of SQ 29,852 [(S)-1-[6-amino-2-[[hydroxy (4-phenylbutyl) phosphinyl]oxy]-1-oxohexyl]-L-proline; 30-40 mg/kg per day], captopril (30-40 mg/kg per day), hydralazine hydrochloride (10-15 mg/kg per day) and a 33% fish meal diet on the prevention and therapy of malignant hypertension were examined. Drugs and diet were given separately, beginning at weaning, maturity or adulthood. Observed effects included antihypertension, prolonged life span and prevention and/or reversal of angionecrosis. Each treatment resulted in an antihypertensive effect, but some adult rats seemed treatment-resistant. SQ 29,852 was the most effective treatment for reducing blood pressure. The life span of animals in the treated groups was extended significantly beyond that of the controls. In particular, those rats treated with either captopril or SQ 29,852 lived in excess of 500 days. This included not only those in which treatment resulted in a lowering of blood pressure, but also those whose severe hypertension was not so reduced. Angionecrosis was observed in the organs of many of the non-treated animals, including the brain, heart, kidneys and testes. Both hydralazine and the fish meal diet had a limited effect, if any, on the prevention or reversal of angionecrosis. In contrast, almost none of the rats given either captopril or SQ 29,852 showed cerebrovascular lesions or angionecrosis of the brain, heart and kidneys; angionecrosis in adult M-SHRSP kidneys disappeared within 10 or 18 days after the initiation of SQ 29,852 or captopril, respectively. This data seems to support a possible role for these two drugs not only in prevention, but also in repair, of angionecrosis independent of markedly high blood pressure in M-SHRSP. Based on our overall observations, SQ 29,852 was seen as the most effective of the treatments studied.

Angiotensin-Converting Enzyme Inhibitors↗
PubMed1990

Distribution and classification of acylphosphatase isozymes.

Distributions of acylphosphatase isozymes among organs of several animal species were investigated. Organ extracts of pig and chicken were treated with isozyme-specific antibodies, subjected to electrophoresis on a polyacrylamide gel, then the gel was stained for acylphosphatase activity. Both animals showed three activity bands; one band was named common type isozyme because of its wide distribution in testis, muscle, brain, heart, spleen, kidney, liver, and erythrocyte, and the other two bands were named muscle type isozymes because of their localization in skeletal muscle. This classification was supported by selective and quantitative reactions of the isozymes to the isozyme-specific antibodies. Because the two bands of the muscle type have the same amino acid sequence and differ only in modifications on an -SH group, it is suggested that pig and chicken have only the two major types of acylphosphatase. This conclusion was supported by similar experiments on dog, human, rabbit, and pigeon.

Acid Anhydride Hydrolases↗
PubMed1989

Activity staining of acylphosphatase after gel electrophoresis.

Acylphosphatase is an ubiquitous enzyme found in a variety of mammalian and avian tissues. Two isozymes of different amino acid sequence have been found in human, chicken, pig, and horse. To survey the distribution of the acylphosphatase isozymes among animal species and tissues, we have developed an activity staining procedure for the enzyme after electrophoresis on a polyacrylamide gel. Tissue extracts of pigs were subjected to electrophoresis, then the gel was stained for acylphosphatase activity in a solution containing acetyl phosphate and lead nitrate. Three activity bands were observed: the slowest moving one, which coincided with that of purified testis acylphosphatase, was widely distributed in testis, muscle, brain, heart, spleen, kidney, liver, and erythrocyte; the other two bands, which coincided with monomer and dimer of purified muscle acylphosphatase, were relatively localized in skeletal muscle.

Acid Anhydride Hydrolases↗
PubMed1989

Ontogenic expression of the two isozymes, Ch1 and Ch2, of chicken muscle acylphosphatase.

Activities of the two isozymes, Ch1 and Ch2, of chicken muscle acylphosphatase were measured in breast muscles, leg muscles, and livers of developing chicks from day 11 in ovo to day 15 of free life. Measurement was performed using rabbit antibodies which could selectively precipitate Ch1 or Ch2. The activity contents of both Ch1 and Ch2 in muscles were low before hatching but rapidly increased after hatching. Ch1 showed a more marked increase than Ch2. In liver, on the other hand, the activity contents of Ch1 and Ch2 remained low throughout the period of pre- and post-hatching.

Acid Anhydride Hydrolases↗
PubMed1989

[A study on maternal humoral immune responses to villous trophoblast using Epstein-Barr virus].

To determine whether or not maternal antibodies are generated during pregnancy, B lymphocytes from puerperal women were transformed using Epstein-Barr virus (EBV). Four weeks after infection with EBV human immunoglobulin (Ig) levels were measured in the culture supernatants by ELISA. In most wells infected B lymphocytes produced a great amount of Ig. The reaction of the culture supernatants from Ig-produced wells with placental tissues of their own was examined by immunohistochemically (by an indirect immunoperoxidase technique). The second layer antibody, goat anti-human Ig peroxidase conjugate was diluted to such a concentration that it did not react to placenta sections without the first layer, that is, culture supernatants. Some of supernatants were found to have IgM which reacted to syncytiotrophoblast. Such positive staining was observed in three of ten multiparous women and in one of two primigravidas. In conclusion, it seems likely that normal pregnant women recognize trophoblasts of their own and make antibodies to them.

Antibody Formation↗
PubMed1988

Purification and characterization of alpha 1-thiol proteinase inhibitor and its identity with kinin- and fragment 1.2-free high molecular weight kininogen.

1. alpha 1-Thiol proteinase inhibitor (alpha 1 TPI) purified from outdated human plasma was a glycoprotein with Mr 83,000 and was composed of heavy and light chains held together with a disulfide bond. 2. The data on amino acid composition, amino terminal sequence of the light chain and carboxyl terminal sequences of the heavy and light chains indicate that alpha 1 TPI is identical with kinin- and fragment 1.2-free HMW kininogen. 3. Purified human plasmin generated a derivative having the same molecular weight (Mr 83,000), same subunit structure (heavy and light chains) and same inhibitory capacity as alpha 1 TPI from HMW kininogen and kinin-free HMW kininogen. This indicated the possibility that alpha 1 TPI is derived from HMW kininogen by plasmin.

Amino Acids↗
PubMed1987

The primary structure of chicken muscle acylphosphatase isozyme Ch1.

The amino acid sequence of chicken muscle acylphosphatase isozyme Ch1 was determined. The protein consists of 102 amino acid residues, does not contain histidine, and the NH2-terminus is acetylated: Ac-Ser-Ala-Leu-Thr-Lys-Ala-Ser-Gly-Ser- Leu-Lys-Ser-Val-Asp-Tyr-Glu-Val-Phe-Gly-Arg-Val-Gln-Gly-Val-Cys-Phe-Arg- Met- Tyr-Thr-Glu-Glu-Glu-Ala-Arg-Lys-Leu-Gly-Val-Val-Gly-Trp-Val-Lys-Asn- Thr- Ser-Gln-Gly-Thr-Val-Thr-Gly-Gln-Val-Gln-Gly-Pro-Glu-Asp-Lys-Val-Asn-Ala- Met- Lys-Ser-Trp-Leu-Ser-Lys-Val-Gly-Ser-Pro-Ser-Ser-Arg-Ile-Asp-Arg-Thr-Lys- Phe-Ser- Asn-Glu-Lys-Glu-Ile-Ser-Lys-Leu-Asp-Phe-Ser-Gly-Phe-Ser-Thr-Arg-Tyr-OH. This sequence differs in 44% of the total positions from the other isozyme (Ch2) of chicken muscle acylphosphatase (Ohba et al., the accompanying paper). The sequence of Ch1 has three substitutions from that of turkey muscle acylphosphatase; these are Ser from Ala at position 9, Ser from Arg at 47, and Lys from Asn at 83. The sequence has about 80% homology with those mammalian muscle acylphosphatases.

Acid Anhydride Hydrolases↗
PubMed1987

The primary structure of chicken muscle acylphosphatase isozyme Ch2.

The amino acid sequence of one, Ch2, of the two isozymes of chicken muscle acylphosphatase was determined. It consists of 98 amino acid residues with N-acetylalanine at the amino(N)-terminus and contains no cysteine: Ac-Ala-Gly-Ser-Glu- Gly-Leu-Met-Ser-Val-Asp-Tyr-Glu-Val-Ser-Gly-Arg-Val-Gln-Gly-Val-Phe-Phe- Arg- Lys-Tyr-Thr-Gln-Ser-Glu-Ala-Lys-Arg-Leu-Gly-Leu-Val-Gly-Trp-Val-Arg-Asn- Thr- Ser-His-Gly-Thr-Val-Gln-Gly-Gln-Ala-Gln-Gly-Pro-Ala-Ala-Arg-Val-Arg-Glu- Leu- Gln-Glu-Trp-Leu-Arg-Lys-Ile-Gly-Ser-Pro-Gln-Ser-Arg-Ile-Ser-Arg-Ala-Glu- Phe- Thr-Asn-Glu-Lys-Glu-Ile-Ala-Ala-Leu-Glu-His-Thr-Asp-Phe-Gln-Ile-Arg-Lys- COOH. The sequence differs in 44% of the total positions from the other isozyme, Ch1. Comparison of the sequence and the predicted conformational profile of Ch2 with those of Ch1 suggests that they share a common evolutionary origin and appear to have retained similar conformations throughout their evolutionary development.

Acid Anhydride Hydrolases↗
PubMed1987

Purification and properties of porcine testis acylphosphatase.

Acylphosphatase has been purified from porcine testis and its properties were compared with those of porcine skeletal muscle acylphosphatase. The molecular weight of the testis enzyme was found to be 10,600, similar to that of porcine skeletal muscle acylphosphatase, on sedimentation equilibrium analysis. The specific activity of the testis enzyme was 10,800 mumol/min/mg at 25 degrees C with benzoyl phosphate as substrate, i.e., higher than that of the muscle enzyme, 7,200 mumol/min/mg, under the same conditions. The pI of the testis enzyme was 8.3, i.e., lower than that of the muscle enzyme, 10.6. There were marked differences in the amino acid compositions of the two enzymes. In particular two histidine residues were present in the testis enzyme but none were present in the muscle enzyme, and no cysteine residue was present in the testis enzyme but one was present in the muscle enzyme. The carboxyl terminal amino acid of the testis enzyme seemed to be lysine, while that of the muscle enzyme is tyrosine. The peptide maps of the testis and muscle enzymes indicated considerable differences in the amino acid sequences of the two enzymes. Differences in the antigenic structures of the two enzymes were demonstrated on enzyme linked immunoassaying and double immunodiffusion. These results indicate that the porcine testis acylphosphatase is an isozyme different from the porcine skeletal muscle acylphosphatase.

Acid Anhydride Hydrolases↗
PubMed1987

Isozymes of isocitrate dehydrogenase from an obligately psychrophilic bacterium, Vibrio sp. strain ABE-1: purification, and modulation of activities by growth conditions.

Each of the two isozymes, which are different in thermostability and quaternary structure, of isocitrate dehydrogenase (NADP+) [IDH: EC 1.1.1.42] was purified to an electrophoretically homogeneous state from an obligately psychrophilic marine bacterium, Vibrio sp. strain ABE-1. Hydrophobic chromatography was an efficient procedure to separate the two isozymes from each other. The isoelectric points of isozyme I (IDH-I; a dimer, Mr 88,100) and isozyme II (IDH-II; a monomer, Mr 80,500) were found to be pH 4.9 and 5.2, respectively. The two isozymes were similar in amino acid compositions, though there were slight differences in the contents of nonpolar and hydroxyl amino acids. However, their NH2-terminal amino acid sequences and immunochemical properties were clearly different from each other. The NH2-terminal amino acid sequence analysis also indicated that the subunits of IDH-I are chemically identical or highly homologous. Non-immuno-crossreactivity between the isozymes enabled us to measure the intracellular contents of the isozymes. IDH-I and -II were found to be differentially regulated in vivo by various growth conditions. IDH-I was induced by acetate, while IDH-II remained almost unchanged.

Acetates↗
PubMed1987

[A study on UFT concentration in tissues and serum of patients with malignant gynecologic tumors following oral administration].

UFT was orally given at a dose of 200 mg twice a day to seven female patients with malignant gynecological tumors. Measurements of blood and tissue concentrations of tegafur (TF), fluorouracil (FU) and uracil (U) showed that the concentrations of both FU and U were clearly increased. The ratio of concentration in the tumor to that in peripheral blood was 9.3, while that of the concentration in the internal iliac lymph nodes to that in the internal iliac artery was 11.2. The changes in blood levels of the three compounds were determined one and five days after UFT administration. There was a distinct difference in the blood levels of the drug among TF, FU and U. TF reached its peak concentration two hours after breakfast and four hours after supper; both FU and U reached their peak concentrations two hours after breakfast and one hour after supper. Furthermore, TF showed a tendency to accumulate after continuous administration, but this was not the case with FU or U. These findings suggest that even during continuous administration, the blood level of FU remains low.

Administration, Oral↗
PubMed1986

Chemical modification of arginine residues of porcine muscle acylphosphatase.

Acylphosphatase (acylphosphate phosphohydrolase, EC 3.6.1.7) from porcine skeletal muscle is inactivated by phenylglyoxal following pseudo-first-order kinetics. The dependence of the apparent first-order rate constant for inactivation on the phenylglyoxal concentration shows that the inactivation is also first order with respect to the reagent concentration. Among the competitive inhibitors for the enzyme examined, inorganic phosphate and ATP almost completely, and Cl- partially, protect the enzyme against the inactivation. The dissociation constants for inorganic phosphate and ATP determined from protection experiments by these inhibitors agree well with those from inhibition experiments by them. These results support the idea that the modification occurs at the phosphate-binding site. The amino-acid analysis reveals the lack of reaction at residues other than arginine. Circular dichroism spectra of the modified enzymes show that the inactivation seems not to be due to denaturation of the enzyme resulting from the modification of the non-essential arginine residues. The relationship between the loss of the enzyme activity and the number of arginine residues modified in the presence and absence of ATP shows that one arginine residue is possibly responsible for the inactivation of acylphosphatase.

Acid Anhydride Hydrolases↗
PubMed1986

Antigenic structure of adenylate kinase from porcine skeletal muscle. IV. Two antigenic determinants on carboxyl-terminal peptide 126-194.

Delineation of the location(s) of antigenic activity in CNBr peptide 126-194 from porcine skeletal muscle adenylate kinase (AK) was attempted. Peptide 126-194 was digested with chymotrypsin, Staphylococcus aureus V8 protease and trypsin, and several short peptides were purified from the digests by reverse-phase high-performance liquid chromatography (HPLC). Inhibition of the binding of radioiodinated peptide 126-194 to goat antibody to porcine skeletal muscle AK (anti-AK antibody) by the peptides obtained by the enzymatic cleavages was examined by solid phase radioimmunoassay (RIA). At least two antigenic determinants have been identified from the results. One is in the amino (N)-terminal half region 126-154, especially in the vicinity of 131-144, and the other is in the carboxyl (C)-terminal half region 165-183, especially in the vicinity of 165-171. Both of them seem to correspond to exposed and accessible regions in the three-dimensional structure of AK. The correlation between antigenicity and high mobility of the loop in the estimated antigenic region 131-144 is also discussed.

Adenylate Kinase↗
PubMed1985

Amino acid sequence of acylphosphatase from porcine skeletal muscle.

The amino acid sequence of acylphosphatase from porcine skeletal muscle was determined. It consists of 98 amino acid residues with N-acetylserine at the amino (N)-terminus: Ac-Ser-Thr-Ala-Arg-Pro-Leu-Lys-Ser-Val-Asp-Tyr-Glu-Val-Phe-Gly -Arg-Val-Gln-Gly-Val-Cys-Phe-Arg-Met-Tyr-Thr-Glu-Asp-Glu-Ala-Arg-Lys-Ile -Gly-Val-Val-Gly-Trp-Val-Lys-Asn-Thr-Ser-Lys-Gly-Thr-Val-Thr-Gly-Gln -Val-Gln-Gly-Pro-Glu-Glu-Lys-Val-Asn-Ser-Met-Lys-Ser-Trp-Leu-Ser-Lys -Ile-Gly-Ser-Pro-Ser-Ser-Arg-Ile-Asp-Arg-Thr-Asn-Phe-Ser-Asn-Glu-Lys- Thr-Ile-Ser-Lys-Leu-Glu-Tyr-Ser-Asn-Phe-Ser-Ile-Arg-Tyr-OH. This sequence has three substitutions of amino acid residues, i.e., Thr/Ala, Ile/Val, and Ile/Val at positions 26, 68, and 96, respectively, from that of horse muscle acylphosphatase, formerly the only mammalian acylphosphatase with known sequence.

Acid Anhydride Hydrolases↗