Rubredoxin was purified from Desulfovibrio vulgaris Miyazaki. It was sequenced and some of its properties determined. Rubredoxin is composed of 52 amino acids. It is highly homologous to that from D. vulgaris Hildenborough. Its N-terminal methionyl residue is partially formylated. The millimolar absorption coefficients of the rubredoxin at 489 nm and 280 nm are 8.1 and 18.5, respectively, and the standard redox potential is +5 mV, which is slightly higher than those of other rubredoxins. Rubredoxin, as well as cytochrome c-553, was reduced with lactate by the action of lactate dehydrogenase of this organism, and the reaction was stimulated with 2-methyl-1,4-naphthoquinone. It is suggested that rubredoxin, in collaboration with membranous quinone, functions as a natural electron carrier for cytoplasmic lactate dehydrogenase of this organism, whereas cytochrome c-553 plays the same role for periplasmic lactate dehydrogenase.

Amino Acid Sequence↗

PubMedDate not supplied

Retroperitoneal malignant fibrous histiocytoma surgically removed six times using a harmonic scalpel.

This paper describes a patient with retroperitoneal malignant fibrous histiocytoma who underwent surgical removal of the tumor 6 times. It is difficult to remove locally recurrent retroperitoneal malignant fibrous histiocytoma many times by repeat surgery, since the tumor tends to adhere tightly to the surrounding scar tissue. In the 5th and 6th operations we conducted on the patient, a harmonic scalpel was useful for separating the tumor from the scar tissue at the previous surgical site.

Cicatrix↗

PubMedDate not supplied

Molecular characteristics of the N-terminal region of the quail follitropin receptor.

We determined the primary structure of follitropin receptor (FSH-R) at its N-terminal extracellular domain, which is the key region of specific hormone binding in avian (quail) species. In this region, quail FSH-R showed about 70% homology with mammalian FSH-Rs at the level of predicted amino acid sequences. The leucine-rich repetitive motif which is conserved in all mammalian FSH-Rs was also detected in the quail FSH-R. However, some unique amino acid replacements were found at the positions of cystein residues and potential N-linked glycosylation sites. The sequence of the quail lutropin receptor (LH-R) previously defined by us showed a homology between FSH-R and LH-R of 47.4%. This value is close to those between mammalian FSH-Rs and LH-Rs, which in the corresponding region are human, 50.3%; rat, 50.9%.

Amino Acid Sequence↗

PubMedDate not supplied

A specific Thy-1 molecular epitope expressed on rat mesangial cells.

An experimental model of proliferative glomerulonephritis induced by antibodies against the Thy-1 antigen has been established and used to study the pathological sequence from mesangiolysis to mesangial proliferation. However, the functional role of the Thy-1 molecule distributed on rat glomerular mesangial cells remains unknown, so the present study was undertaken to determine the precise subcellular localization of Thy-1 molecules in vitro using two anti-Thy-1 monoclonal antibodies, 1-22-3 and OX-7. Immunofluorescence and immunoelectron microscopic studies in combination with laser scanning analysis showed that the localization of 1-22-3 and OX-7 bound to cultured rat mesangial cells differed, particularly when cocultured with vascular endothelial cells. An epitope recognized by 1-22-3 was concentrated specifically on the mesangial cell surfaces facing the neighboring endothelial cells. In contrast, OX-7 bound to mesangial cell surfaces and extracellular parts in a diffuse pattern independent of contact with endothelial cells. This finding is consistent with our previous ultrastructural study in which the reactivity of 1-22-3 with normal kidney tissue was limited to mesangial cell surfaces facing endothelial cells. These results led us to conclude that the specific Thy-1 molecular epitope recognized by 1-22-3 is associated with points anchoring mesangial and endothelial cells, where this anti-Thy-1 antibody binds after injection in vivo, resulting in mesangial cell detachment from the vascular capillary wall, mesangiolysis and mesangial cell dysfunction. We believe that the critical epitope detected by 1-22-3 in this study plays an important role in mesangial cell function and injury.

Animals↗