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Biomedical subjects

T Azuma

Publications and source records attributed to T Azuma.

At least 415 records · Page 23Linked to original sources
PubMed1978

Monomer-dimer equilibria of a Bence Jones protein and its variable fragment.

The circular dichroic (CD) spectra of a type lambda Bence Jones protein (Tod), its variable (VL) fragment, and the constant (CL) fragment of a type lambda protein (Nag) were measured under various conditions. In the pH region from 5.5 to 7.5, the CD spectra of Tod protein with intact interchain disulfide bond (L(SS)) and and CL did not change with pH, while the spectra of Tod protein in which the interchain disulfide bond had been reduced and alkylated (L(RA)) and VL did not change with pH. The dimerization reactions of L(RA) and VL were studied by following the CD change with protein concentration. The CD spectrum of CL did not change with the protein concentration. The dimerization constant for L(RA) was 4 X 10(4) M-1 at at pH 7.5 and 25 degrees C, which was smaller than that for VL (1 X 10(5) M-1). The ellipticity at 278 nm for the L(RA) dimer was different from that for the L(SS) dimer and changed with pH. These findings indicate that the L(RA) dimer and L(SS) dimer have different conformations. The differences in the conformation and L-L interaction between the L(RA) dimer and L(SS) dimer are discussed on the basis of the conformations of VL and CL and the interactions between the paired domains.

Alkylation↗
PubMed1978

Formation of interchain disulfide bonds in Bence Jones proteins and Fab(t) fragments of immunoglobulin G through thiol-disulfide interchange.

The formation of interchain disulfide bonds from partially reduced Bence Jones protein (Nag, type lambda) and Fab(t) fragments of IgG1 myeloma proteins was studied in the presence of various disulfide reagents. The results could be well explained in terms of the scheme proposed previously (Kishida et al. (1976) J. Biochem. 79, 91-105). In this scheme, it was assumed that two kinds of intermediate, which form mixed disulfides with either of the paired thiol groups, are produced. For type lambda Bence Jones proteins, only one of the two intermediates can form the inter L-L disulfide bond. The fraction of intermediate having the ability to form the inter L-L disulfide bond was estimated to be 72% of the total Nag protein and was the same irrespective of the kind of disulfide reagent examined. For Fab(t), on the other hand, both intermediates equally can form the inter Fd-L disulfide bond. On the basis of the results with cystamine, it was shown that the formation of an inter Fd-L disulfide bond from the intermediate proceeds about 100 times as rapidly as that of an inter L-L disulfide bond.

Bence Jones Protein↗
PubMed1978

Isolated, blood-perfused canine arteries: different vasoconstrictor responses of internal and external carotid arteries to 5-hydroxytryptamine.

Canine carotid arteries were isolated, suspended in a bath and perfused under a constant flow rate with arterial blood led from a support dog. Resting perfusion pressure was set at a constant level over 50 mm Hg. Drugs were administered into the endothelial side of the artery through a cannulated tubing and the response was obtained as pressure changes. This preparation was proved to be superior to usual isolated arterial strips, since its reactivity was kept in a stable condition over 5-10 hours at 37 degrees C. Using this preparation, effects of 5-hydroxytryptamine (5-HT) on the internal and external carotid arteries were investigated in comparison with effects of norepinephrine. In the internal carotid artery, 5-HT caused a much more potent vasoconstriction than norepinephrine. On the other hand, in the external carotid artery, 5-HT caused only slight vasoconstriction, while norepinephrine produced a marked vasoconstriction.

Animals↗
PubMed1978

Ionization and reactivities of the thiol groups which participate in the formation of interchain disulfide bonds of Bence Jones proteins and an Fab(t) fragment.

The pK values and reactivities of the thiol groups which participate in the formation of interchain disulfide bonds in Bence Jones proteins and the Fab(t) fragment of a myeloma protein (Jo) (IgGl, kappa) were determined by means of the reactions with chloroacetamide and DTNB, and of spectrophotometric titration. The two thiol groups of partially reduced type kappa Bence Jones protein dimers had the same pK values (pK = 9.76 at 0.2 ionic strength and 25 degrees C) and the same true second-order rate constants (k) toward chloroacetamide (k = 18.8 x 10(-2) M-1 . S-1). The two thiol groups of partially reduced type lambda Bence Jones protein dimers had different pK values but the variation of the pK values among the specimens was small (pK1 = 8.5-8.6 and pK2 = 9.5-9.7 at 0.2 ionic strength and 25 degrees C). The spectrophotometric titration of partially reduced Nag protein (type lambda) also showed that the two thiol groups have different pK values. The pK values of two thiol groups of the partially reduced Fab(t) fragment were determined as 8.51 and 9.76 at 0.2 ionic strength and 25 degrees C. The effect of ionic strength on the pK values of the thiol groups of partially reduced Nag protein and the pK values of the thiol groups in partially reduced Ta protein (type kappa) and in a hybrid molecule formed between partially reduced Ta protein and partially reduced and alkylated H chains indicated that the difference in pK values did not arise from electrostatic interaction between the two thiol groups, but that the pK values are intrinsically different. The true rate constants, k1 and k2, of the two thiol groups of type lambda Bence Jones proteins varied with the specimen (k1 = 1.9-5.7 x 10(-2) M-1 . S-1 and k2 = 18.5-25.0 x 10(-2) M-1 . S-1). The k1 and k2 values for Jo-Fab(t) were 7.21 x 10(-2) and 23.1 x 10(-2) M-1 . S-1, respectively. On the basis of these pK values and reactivities, we discuss the reformation of the interchain disulfide bonds from partially reduced Bence Jones proteins and immunoglobulins in the presence of oxidized glutathione.

Acetamides↗
PubMed1977

Noninvasive measurements of digital arterial pressure and compliance in man.

A noninvasive method was developed for measuring the digital arterial pressure and the compliance by using a fingertip pneumoplethysmograph and a pneumatic cuff. The compliance (C) of the digital artery was obtained from the peak amplitude of the volume pulse wave (deltaVp-a) under the effect of the cuff pressure (Po-a) by the equation: C = deltavp-a/(Ps - P-o-a) during the dicrotic phase defined in this study. The normal mean value was 11.37 +/- 0.59 X 10(-5) cm3/mmHg. On lowering of the cuff pressure, the moment when the deltaVp value becomes positive is regarded as the systolic pressure (Ps). At the end of the dicrotic phase, the mean amplitude (deltaVss') of the pulse wave during one pulse cycle (SS') and the ratios (deltaVss'/deltaVsd), where deltaVsd is the mean amplitude of the wave during the systolic period (SD), of successive waves after a particular wave fail to increase at the same rate when the cuff pressure decreased below the diastolic pressure. The cuff pressure corresponding to this particular wave is regarded as the diastolic pressure (Pd). The mean value of the mean digital pressure of normotensive subjects was 80.6 +/- 1.2 mmHg.

Arteries↗
PubMed1977

Protein clearances in chronic renal failure: a contribution to the pathophysiology of tubular dysfunction.

Glomerular selectivity is still conserved in chronic renal failure (CRF), although it is poor when compared with non-CRF. In addition, clearances per unit nephron of 15 plasma proteins (Cprot./Ccr X 100) are markedly elevated in CRF. This reflects an effect of osmotic diuresis on tubular reabsorption of proteins, which may partially account for the tubular dysfunction shown by the augmented excretion of the low molecular proteins, such as lysozyme and insulin. Besides this, there exists certainly tubular damage, since tubuloglomerular protein ratio (Clysozyme/Ctransferrin) rises with the progress of glomerular injury.

Albumins↗