Effect of Gender Differences on Transplant Kidney Function.

BACKGROUND: Transplant kidney function is thought to be affected by sex differences, such as physical conditions including muscle volume, sex hormones, immune responses, and so forth. We examined the effect of sex differences on transplant kidney function. METHODS: The subjects were selected from kidney transplant recipients, who received kidney transplantation on our hospital between January 2000 and August 2015. Cadaveric donors and parent-child pairs with an age difference were excluded, then we included 47 recipients whose sex was different from the sex of the donor. We compared transplant kidney function between male donors and female recipients group (M→F, n = 20) and female donors and male recipients group (F→M, n = 27). RESULTS: Nadir creatinine value was higher in the F→M group than in the M→F group (1.09 mg/dL vs 0.76 mg/dL, P < .0001). The estimated glomerular filtration rate (eGFR) was significantly higher in the M→F group than in the F→M group (66.6 mL/min/1.73 m2 vs 50.1 mL/min/1.73 m2, P = .002), and eGFR ratio (recipient to donor) was significantly higher in the M→F group than in the F→M group (1.13 vs 0.57, P < .0001). Multiple linear regression analysis showed that the only the sex of the recipient was significant prognostic factor of eGFR after renal transplantation (P = .037). CONCLUSIONS: The short-term kidney function of the graft from male to female was better than that of the graft from female to male.

Properties of the peptides liberated from rice protein in sokujo-moto.

In the supernatant of sokujo-moto, a high level of acid carboxypeptidase (ACP) activity and a large amount of peptides were observed, however, the amount of free amino acids liberated was small. In order to determine why these peptides were not hydrolyzed to any significant degree by the ACP, the properties of the peptides in sokujo-moto were investigated in this study. Peptides were fractionated from sokujo-moto by ion exchange column chromatography. ACP purified from rice-koji (rice overgrown with Aspergillus oryzae) was allowed to react with the peptides, and it was found that they were not hydrolyzed to any significant degree by the enzyme. Gel filtration chromatography was performed to ascertain the molecular size distribution of the peptides in sokujo-moto, and it was revealed that they were of low molecular sizes; molecular size: mainly in the range of 200-400, and chain length: 2-3. ACP purified from rice-koji was also allowed to react with various synthetic peptides, and it was found that ACP of rice-koji could not rapidly hydrolyze low-molecular-size peptides, such as dipeptides or tripeptides. Acid protease (AP) purified from rice-koji released peptides of molecular sizes mainly in the range of 300-600 or above from rice protein under acidic conditions (pH 3.6; the pH of sokujomoto). When AP and ACP were allowed to act at the same time on rice protein, mainly low-molecular-size peptides (molecular sizes mainly in the range of 200-400) were produced. From these results, it was estimated that AP released peptides with molecular sizes mainly in the range of 300-600 or above from rice protein and ACP degraded the relatively higher molecular size peptides among them to lower molecular size peptides; consequently only low-molecular-size peptides with molecular sizes mainly in the range of 200-400 were released in the supernatant of sokujo-moto.

Properties of TCA-insoluble peptides in kimoto (traditional seed mash for sake brewing) and conditions for liberation of the peptides from rice protein.

It was found that a large amount of TCA (trichloroacetic acid)-insoluble peptides were liberated into the supernatant of kimoto on the 7th-10th day of mashing. These TCA-insoluble peptides had five polypeptide groups (12, 21, 31, 38, and 55 kDa) on SDS-PAGE (SDS-polyacrylamide gel electrophoresis), and a large amount of high molecular weight peptides, higher than 10,000, were observed upon gel filtration chromatography using TSKgel G2000swxl (Tosoh Co.). Four of these peptides (12, 21, 31, and 38 kDa on SDS-PAGE) appeared specifically in kimoto, and were not detected at all either in sokujo-moto or in the main mash for sake brewing. These TCA-insoluble peptides were fractionated from the supernatant of kimoto on the 9th day, and it was revealed that free amino acids were produced abundantly from them in the presence of the enzyme of rice-koji. Therefore, it was assumed that the peptides are related to the abundant production of free amino acids in kimoto. For the liberation of these TCA-insoluble peptides from rice protein, the enzyme of rice-koji was indispensable. The enzyme liberating the TCA-insoluble peptides from rice protein was purified from rice-koji, and was presumed to be identical with acid protease (AP) of rice-koji. The presence of a high concentration of glucose (higher than 20%) was also indispensable for the liberation of the TCA-insoluble peptides. Furthermore, it was revealed that the peptides were liberated from rice protein under a limited pH of around 4.5.

Influence of amino acid content in seed mash on peptide uptake by yeast cells in main mash in sake brewing process.

It was found that the peptide content of the main mash in the sake brewing process, seeded with kimoto, was higher than in that seeded with sokujo-moto, although the peptide content in kimoto was lower than in sokujo-moto. We investigated the underlying reasons. As a result, we found that the high concentration of free amino acids originating from kimoto decreased the peptide uptake ability of yeast cells in the main mash seeded with kimoto.

Resolution and complementation of the labile L-leucine-pyruvate transaminase. An intermediate during enzyme formation under nitrogen starvation in Gluconobacter suboxydans.

L-Leucine-pyruvate transaminase (mol. wt. 70 000) in Gluconobactersuboxydans synthesized during nitrogen starvation contained a labile form which changed to the stable one later. The labile enzyme (mol. wt. 70 000) dissocated to the two proteinaceous components: a cationic one (mol. wt. 10 000--20 000) and an anionic one (mol. wt. 50 000--60 000), during column chromatography on DEAE-cellulose. The enzyme activity was reconstructed when they were mixed. The reconstructed enzyme had almost the same molecular size and enzymatic properties as the labile and the native stable enzymes.