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H Toda

Publications and source records attributed to H Toda.

At least 181 records · Page 10Linked to original sources
PubMed1985

Amino acid sequence of calmodulin from wheat germ.

The complete amino acid sequence of calmodulin from wheat germ was determined by isolating and sequencing the cyanogen bromide and tryptic peptides. The protein consisted of 149 amino acid residues and its amino(N)-terminus was blocked with an acetyl group. Wheat germ calmodulin lacked tryptophan and contained 1 mol each of histidine, tyrosine, cysteine, and N epsilon-trimethyllysine residues per mol of the protein. A comparison of its amino acid sequence with that of bovine brain calmodulin indicated that there were eleven amino acid subsitutions other than amide assignments, two insertions and one deletion of amino acid residues in wheat germ calmodulin.

Amino Acid Sequence↗
PubMed1984

The genesis of bifid T waves: experimental demonstration in isolated perfused rabbit hearts.

In an attempt to elucidate the genesis of bifid T waves, we recorded transmembrane potentials of subepicardial ventricular muscle fibers simultaneously with a bipolar ventricular electrogram in isolated, perfused rabbit hearts, and the timing of the two apices of the T wave (aT1, aT2) was correlated with ventricular repolarization. The following results were obtained. (1) In seven of the nine hearts in which the repolarization process was mapped on the anterior and posterior surfaces of both ventricles, the 80% repolarization times of the left and the right ventricles were scattered around aT1 and aT2, respectively, and their average values closely corresponded to Q-aT1 and Q-aT2 intervals. This suggested that aT1 and aT2 depended on repolarization of the left and the right ventricles, respectively. (2) In one heart, aT1 appeared to reflect repolarization of the posterior ventricular wall, and aT2 that of the anterior wall. (3) In the remaining heart, aT2 coincided with repolarization of the anterobasal portion of the right ventricle, and aT1 that of the remaining portions of the ventricles. Even when ventricular repolarization was modified by low K+, low Ca2+ or procainamide perfusion, or by premature atrial stimulation, the close temporal correlation of the left and right ventricular repolarization with the two apices of the T wave was maintained. Selective cooling of the perfusate in either the left or the right coronary artery resulted in the production of bifid T waves in which aT2 coincided with the delayed repolarization of the cooled ventricle. We conclude that either physiologically or pathologically delayed repolarization in certain portions of the ventricles is most likely the cause of bifid T waves.

Action Potentials↗
PubMed1984

Relation between QT interval and heart rate. applications and limitations of Bazett's formula.

We studied the relationship between QT interval and RR interval when the heart rate was changed by atrial pacing, atropine, isoproterenol, and exercise in nine healthy adult males. The following results were obtained: (1) QT shortening with an increase in heart rate was minimal in atrial pacing and an equation QT = k4 square root RR was obtained from the QT-RR relationship during atrial pacing (r = 0.64, p less than 0.001); (2) shortening of QT with shortening of RR was least in atrial pacing; (3) during recovery from exercise it was largest and almost coincident with Bazett's formula; (4) Bazett's formula, therefore, is clearly applicable in the evaluation of ECGs recorded at rest or after exercise; (5) Bazett's formula can not be applied in the evaluation of an effect of some drug or maneuver on the QT when such a drug or maneuver can affect both the QT and the RR directly. The RR-dependent QT change can be estimated from the equation QT = k4 square root RR and the difference between a measured QT and the estimated RR-corrected QT would be a genuine effect of the drug or maneuver on the QT at that heart rate. We conclude that atropine, isoproterenol and exercise actually shorten the QT interval.

Adolescent↗
PubMed1984

Clinical electrocardiographic studies of bifid T waves.

In 129 electrocardiograms from 129 patients showing bifid T waves as well as U waves the intervals from the beginning of the QRS complex to the two T wave apices (QaT1, QaT2), to the end of the T wave (QeT), and to the apex of the U wave (QaU) were measured. Eighty additional electrocardiograms from matched control subjects showing single peaked T waves were also studied. The precordial distribution of bifid T waves was assessed by calculating lead prevalence indices. This index progressively increased from 2.15 in the age range 20-29 years to 3.72 in the age range 60-69 years, and was significantly higher in patients with left ventricular hypertrophy and ischaemia (4.04) than in those with otherwise normal electrocardiograms (2.35). Thus older age and left ventricular pathology were accompanied by a more leftward location of bifid T waves. Exercise accentuated the bifid nature of the T wave in 12 of 18 patients with otherwise normal electrocardiograms, and diminished it in 11 of 19 cases with left ventricular hypertrophy and ischaemia. When 41 otherwise normal tracings showing bifid T waves were compared with those of 42 matched controls showing single peaked T waves, the QTc was longer and the eTaU interval shorter in the group with bifid T waves. Similarly, 40 patients with left ventricular hypertrophy and ischaemia showing bifid T waves had longer QTc and shorter eTaU intervals than 38 patients with the same diagnosis with single peaked T waves. These findings suggest that right precordial bifid T waves in younger patients with otherwise normal electrocardiograms probably result from delayed right ventricular repolarisation, whereas left precordial bifid T waves in older patients with left ventricular hypertrophy and ischaemia may indicate repolarisation delay in the ischaemic left ventricle.

Adult↗
PubMed1982

Isolation and characterization of Taka-amylase A apoprotein deglycosylated by digestion with almond glycopeptidase immobilized on Sepharose.

Taka-amylase A (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1), which contains a single asparagine-linked oligosaccharide unit, was digested with almond glycopeptidase immobilized on Sepharose 6B at 20 degrees C for 4 h. A maximum of 10% of the parent protein was isolated as apoprotein by column chromatography on Con-A Sepharose. The characteristics of the apoprotein were compared to those of the native Taka-amylase A. The removal of the sugar chain from Taka-amylase. A caused no change in the pH-activity profile or in kinetic parameters of the hydrolysis of soluble starch. The stability of the apoprotein toward changing pH and digestion by proteases did not show any appreciable difference from that of the native Taka-amylase. These results suggest that the carbohydrate moiety of Taka-amylase A is not an essential participant in the catalysis.

Amidohydrolases↗
PubMed1982

Amino acid sequence of beta 2-bungarotoxin from Bungarus multicinctus venom. The amino acid substitutions in the B chains.

beta 2-Bungarotoxin (beta 2-toxin) was isolated from the venom of Bungarus multicinctus by means of CM-Sephadex C-25 column chromatography, Sephadex G-75 gel filtration and CM-Sephadex C-25 column rechromatography. beta 2-Toxin consisted of two dissimilar polypeptides, a (120 amino acid residues) and B (60 amino acid residues) chains, crosslinked by an interchain disulfide bond. The neurotoxicity (LD50) and phospholipase activity of beta 2-toxin were 0.029 micrograms/g of mouse and 48.9 units/mg of toxin, respectively, and both the activities were slightly weaker than those (0.019 micrograms/g and 60.9 units/mg) of beta 1-bungarotoxin (beta 1-toxin). beta 2-Toxin was reduced and carboxymethylated and then its RCM-A and -B chains were separated. Each RCM-chain was maleylated and then digested with TPCK-trypsin. The tryptic peptides were sequences by manual Edman degradation or the dansyl-Edman method, and the total alignment of the tryptic peptides from each RCM-chain was deduced based on the amino acid sequences of the A and B chains of beta 1-toxin. The amino acid sequence of the B chain of beta 2-toxin differed from that of the B chain of beta 1-toxin by 22 amino acid substitutions, while those of their A chains were identical. We concluded that the variation in the amino acid sequence of the B chains did not significantly affect the neurotoxicity of the beta-toxins. The amino acid sequences of the B chains of the two beta-toxins were homologous to those of proteinase inhibitors from snake venoms and mammalian pancreas, but no inhibitory activity of the two beta-toxins on proteinases was observed.

Amino Acid Sequence↗
PubMed1982

Amino acid sequences of three beta-bungarotoxins (beta 3-, beta 4-, and beta 5- bungarotoxins) from Bungarus multicinctus venom. Amino acid substitutions in the A chains.

The two most basic beta-bungarotoxins (beta 3- and beta 4-toxins) and another, less neurotoxic beta-bungarotoxin (beta 5-toxin) were purified from Bungarus multicinctus venom, by a combination of CM-Sephadex C-25 column chromatography and Sephadex G-75 gel filtration. The three toxins consisted of two dissimilar polypeptides (A chain, 120 amino acid residues; B chain, 60 residues). The LD50 values of the beta 3- and beta 4-toxins were 0.066 micrograms and 0.072 micrograms/g of mouse, respectively, and their phospholipase A activities were 43.2 and 36.5 units/mg of toxin, respectively. beta 5-Toxin was weaker in neurotoxicity (LD50, 0.13 micrograms/g of mouse) than the others, and its phospholipase activity was 47.6 units/mg of toxin. Each toxin was separated into RCM-A and RCM-B chains after reduction and S-carboxymethylation. The RCM-polypeptides were maleylated and digested with TPCK-trypsin. The tryptic peptides were sequenced with manual Edman degradation or the dansyl-Edman method. The final alignment of the tryptic peptides from the respective RCM-polypeptides was deduced on the basis of the amino acid sequences of the A and B chains of beta 1-bungarotoxin (beta 1-toxin). The amino acid sequences of the A chains of the beta 3- and beta 4-toxins were identical but differed from those of the A chains of the beta 1- and beta 2-toxins by 4 amino acid substitutions in the COOH-terminal portions (residues 109-120) and substitution at position 87. The amino acid sequences of the B chains of the beta 3- and beta 4-toxins differed from each other, but they were identical with those of the B chains of the beta 1- and beta 2-toxins, respectively. The amino acid sequence of the A chain of beta 5-toxin differed from that of the A chain of beta 1-toxin by consecutive substitutions in residues 55-60 and substitutions at positions 23, 87, and 89. The amino acid sequence of the B chain of beta 5-toxin was identical with those of the B chains of beta 1- and beta 3-toxin. From our results on the effects of the amino acid displacements found in the A chains on the neurotoxicity, it was concluded that the COOH-terminal portion in the A chains was not essential to their neurotoxicity, whereas the region of residues 55-60 in the A chains appeared to participate in the constitution of the neurotoxically active site of the beta-toxins.

Amino Acid Sequence↗
PubMed1981

Electrocardiographic changes induced by the stellate ganglion block in normal subjects.

In order to examine the laterality of the sympathetic control of the human heart, electrocardiographic changes induced by a unilateral stellate ganglion block (SGB) were observed. 10ml of 1% lidocaine was used for the block and post-block ECG was recorded just after the appearance of Horner's sign. Patients who developed vocal hoarseness were excluded. 15 recordings of 14 subjects with right SGB and 16 recordings of 12 subjects with left SGB were used for analysis. A significant increase in the P-P interval from 0.90 +/- 0.17 sec to 0.96 +/- 0.16 sec. was observed only with right SGB and the predominance of the right side in the sympathetic nervous control of the human heart was thus demonstrated. The atrioventricular conduction time was not affected by either the right or left SGB. The QTc was slightly but significantly prolonged only by the right SGB, from 0.40 +/- 0.04 sec. to 0.43 +/- 0.04 sec. This prolongation was not large enough to support a definite conclusion and further investigations should be made.

Adult↗
PubMed1981

Purification and characterization of phospholipase A from Bungarus multicinctus venom.

Phospholipase A was purified 16.3-fold in terms of specific activity from the venom of Bungarus multicinctus by ion exchange chromatography on a CM-Sephadex C-25 column followed by gel filtration on a Sephadex G-75 column. The overall enzyme yield was 3.5% from the crude venom. The molecular weight and isoelectric point of the purified enzyme were estimated to be 14,000 and 7.9 by electrophoresis on SDS-polyacrylamide gel and on polyacrylamide gel for isoelectric focusing, respectively. The enzyme was a single polypeptide chain consisting of 118 amino acids. Its N- and C-terminal residues were asparagine and glutamine, respectively. The enzyme was stable in the pH range of 2--10 and retained full activity after incubation for 24 h at 37 degrees C. The optimum hydrolysis of egg yolk phosphatidyl choline was observed at pH 8.5 and the specific activity was 1,450 units per mg of the enzyme. The enzyme was inactivated by treatment with p-bromophenacyl bromide, accompanied by the loss of one of two histidine residues.

Amino Acid Sequence↗
PubMed1981

Amino acid sequence of phospholipase A from Bungarus multicinctus venom.

Bungarus multicinctus phospholipase A was reduced and carboxymethylated. The RCM-enzyme was digested with TPCK-trypsin or cleaved with cyanogen bromide followed by chymotrypsin digestion. The resulting peptide mixtures were fractionated by gel filtration on Sephadex G-50 and G-25 columns or by DEAE-cellulose (DE-32) column chromatography. Further purification of the peptide mixtures was performed by paper electrophoresis at pH 3.5 or 6.5 or by paper chromatography. The sequences of isolated peptides were determined by the manual Edman or dansyl-Edman method. From the sequences of these peptides the whole enzyme sequence (total 118 residues) was deduced. The complete sequence of the enzyme is similar to those of phospholipases A2 from other snake venoms and mammalian pancreas. Further, a 58% sequence homology was found between the present phospholipase A and the A chain of beta 1-bungarotoxin, a presynaptic neurotoxin having weak phospholipase A activity, contained in the same venom.

Amino Acid Sequence↗
PubMed1981

Amino acid sequence of calmodulin from scallop (Patinopecten) adductor muscle.

The complete amino acid sequence of scallop calmodulin was determined by isolating and sequencing the peptides obtained after cyanogen bromide cleavage and tryptic digestion. The protein consisted of 148 amino acid residues and its amino(N)-terminus was blocked with an acetyl group. Scallop calmodulin lacked tryptophan and cysteine residues and contained one mol each of N epsilon-trimethyllysine (Tml) and histidine residues per mol of the protein. Scallop calmodulin contained only one tyrosine residue, while vertebrate calmodulins contain two. On comparing its amino acid sequence with that of bovine calmodulin, three amino acid substitutions were found at positions 99(Tyr leads to Phe), 143(Gln leads to Thr), and 147(Ala leads to Ser).

Amino Acid Sequence↗
PubMed1980

Molecular structure of taka-amylase A. I. Backbone chain folding at 3 A resolution.

The crystal structure of Taka-amylase A was studied by an X-ray diffraction method at 3 A resolution. A total of 452 amino acid residues were found from the electron density map at the present stage. The four disulfide bonds and the branched carbohydrate were also located on the map. The difference electron density map of the maltotriose-soaked crystal showed that a maltose unit was bound in the active center left. The binding of iodine atoms to the enzyme was also studied.

Amylases↗