Biomedical subjects

O Minowa

Publications and source records attributed to O Minowa.

43 records · Page 3Linked to original sources

PubMed1984

N-terminal region (domain 1) of calmodulin is the low affinity site for Ca2+. A 13C NMR study of S-cyanocalmodulin.

A single cysteine residue (Cys-27) of wheat calmodulin was labeled with 13C by cyanylation. No change in the Ca2+ saturation pattern was observed after the cyanylation. On titration which Ca2+, the chemical shift of the 13C-label showed a downfield shift. The downfield shift was observed at Ca2+/calmodulin molar ratios between 1.8 and 3.5, while a blue shift of the UV absorption of Tyr-139 was observed between 0 and 1.7. The result indicated the domain 1 containing Cys-27 to be the low affinity site for Ca2+.

Amino Acids↗

PubMed1984

Calcium binding to tryptic fragments of calmodulin.

Fragments of scallop testis calmodulin were prepared by tryptic digestion. One peptide consisted of 75 amino acid residues from N-acetylalanine to lysine at position 75 (F12) and the other of 71 residues from aspartic acid at position 78 to C-terminal lysine (F34). Flow dialysis and equilibrium dialysis experiments revealed the existence of two Ca2+ binding sites in each fragment. Half-saturating concentrations of the Ca2+ titration curves were 11 microM for F12 and 3.2 microM for F34, and Hill coefficients were obtained as 1.14 and 1.84, respectively. The results indicate that the high-affinity sites for Ca2+ are located on the C-terminal region of the calmodulin. The sum of the two Ca2+ titration curves of F12 and F34 fits well to the curves of Ca2+ binding to intact calmodulin. This shows that the characteristic of Ca2+ bindings in intact calmodulin did not change after separation of the whole molecule into two domains, F12 and F34. The domains corresponding to F12 and F34 may exist independently from each other in the intact calmodulin molecule.

Animals↗

PubMed1983

Ca2+-induced conformational changes of 20,000 dalton light chain of vertebrate striated muscle myosins.

The 20,000 dalton light chain (L2) was isolated from rabbit and chicken striated muscle myosins, and the Ca2+-induced conformational changes of these proteins were investigated. 1) The reaction of thiol groups of L2 with dithiobisnitrobenzoic acid (DTNB), 2) measurements of the UV difference absorption spectrum, 3) measurements of Stokes radius (Rs) by gel filtration and 4) measurements of the ESR spectrum of L2 whose cysteine or tyrosine residues were spin-labeled were used for the structural studies. The effect of Ca2+ on phosphorylated L2 was also investigated. The long axis of chicken L2 was calculated as 136A from the Stokes radius, suggesting that the L2 is an asymmetrical molecule. After the addition of Ca2+ the long axis was reduced to 104 A. The same effect of Ca2+ has been reported with rabbit L2 (Alexis, N.M. & Gratzer, W.B. (1978) Biochemistry 17, 2319-2325). Besides this large shape change, the addition of Ca2+ to L2 induced environmental changes around tyrosine residues and also changes in the reactivity of cysteine residues with DTNB. Ca2+ is supposed to be bound to the N-terminal region of the molecule, while the tyrosine and cysteine residues are located at the C-terminal region, which is probably sterically remote from the N-terminal region. The reason for the remote effect of Ca2+ may be related to the structural rigidity of the L2 molecule. The functions of two properties of L2, Ca2+-binding and phosphorylation, are discussed in relation to muscle contraction.

Animals↗

PubMed1983

Divalent cation binding to wheat germ calmodulin.

The Ca2+ binding to plant (wheat germ) calmodulin was measured in 0.1 M NaCl by a flow-dialysis method. The four macroscopic binding constants best fitted to the data were 0.20, 0.25, 0.025, and 0.0024 microM-1. The cysteine residue of this calmodulin is located at the 27th position from the NH2-terminal (Yazawa, M. et al. (1982) Abstr. 33th Conf. Protein Structure pp. 9-12, Osaka). According to the quantitative analysis of the reaction of 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) with Cys 27, the calmodulin which binds 3 Ca2+ showed the minimum reactivity with DTNB. This suggests that the site for the third Ca2+ binding is located close to Cys 27. Cys 27 was spin-labeled with N-(2,2,6,6-tetramethyl-4-piperidine-1-oxyl)maleimide, and its ESR spectrum was measured in the presence of Mn2+ and/or Ca2+. The rotational relaxation time of the label (1.2 ns) was increased by about one-tenth with 1 to 2 mol of bound Ca2+, but was unchanged with Mn2+. On the other hand, Mn2+ induced a remarkable quenching of the spectrum. From the decrease in the peak heights of the ESR spectrum, the distance between the label and the first bound Mn2+ was estimated to be 0.8 nm. It is concluded that the first Mn2+ binds to a domain near the NH2-terminal. The difference UV absorption spectrum induced by Mn2+ was similar to that induced by Ca2+. However, the amount of Mn2+ needed to saturate the difference spectrum was 1 mol more than the amount of Ca2+.(ABSTRACT TRUNCATED AT 250 WORDS)

Binding Sites↗

PubMedDate not supplied

Paratesticular aggressive fibromatosis: CT findings.

Aggressive fibromatoses commonly originate from the musculoskeletal system, mesentery, and retroperitoneum. We report a case of aggressive fibromatosis arising from the spermatic cord. On helical computed tomography, the lesion appeared as a solid mass with well-defined borders in the scrotum and with infiltrative features in the retroperitoneum.

Aged↗

PubMedDate not supplied

Emphysematous pyelonephritis- conversion of type i to type II appearance on serial CT studies.

Recently, emphysematous pyelonephritis (EPN) has been classified into two subtypes based on CT findings. We recently experienced a patient whose CT image changed from type I (extensive destruction of the renal parenchyma with a large amount of air density without any fluid collection) to type II (containing a large amount of fluid) during the course of conservative treatment. We believe that some patients with type I EPN can change to type II EPN.

Disease Progression↗

PubMedDate not supplied

Iodide mumps after contrast enhanced CT with iopamidol: a case report.

We have experienced a case of iodide mumps after CT examination with 100 ml of iopamidol. The patient was a 70-year-old woman with a history of right nephrectomy due to right renal cancer. She underwent CT examination to explore local recurrence and abdominal metastases including lymph node and liver metastases. Three hours after the CT examination, she complained of nausea, vomiting, facial flushing, bilateral jaw pain, and fever. The laboratory findings 12 hours after CT examination showed increased white blood cells and elevated serum amylase enzyme. Analysis of the amylase fraction showed that 86% originated from the salivary glands. She was admitted to the hospital, and the symptoms continued for four days, with decreasing severity. Anti-inflammatory therapy was performed, and the patient was discharged six days after the event.

Aged↗