Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas

In the previous papers^(1.2), we investigated the effects of ACE inhibitory activities of phosphopeptides of P-1 and C-2 which were obtained from edible oyster by proteolytic hydrolyzation. In this investigation, the ACE inhibitory phosphopeptides of T-1 was further purified by ultrafiltration and Sephadex G-15 column chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of T-1-1,T-1-2 and T-1-3 in the pepsin hydrolyzates of the T-1 by gel filtration rechromatography on Sephadex G-15. The inhibition of ACE of the three kinds of phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) was analyzed in vitro. The IC_ values of T-1-1,T-1-2 and T-1-3 of phosphopeptides for ACE were 0.159,0.095 and 0.140 mg protein/ml, respectively. The T-1-2 fraction had the most potent inyhibitory activity and showed 0.095 mg protein/ml inhibition against ACE at IC_ value. It has been demonstrated that the T-1-1,T-1-2 and T-1-3 contained about 33.3%, 3.01% and 27.12% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) were characterized by relatively high percentage for Tyr, Ser, Arg, Ala, Asp and Phe. When the ACE inhibitory phosphopeptides were analyzed by thin layer chromatography, some ninhydrine-positive spots were observed. These results suggest that the phosphopeptides are a mixture of several phosphopeptides

Reducing the environmental impact of surgery on a global scale: systematic review and co-prioritization with healthcare workers in 132 countries

Abstract Background Healthcare cannot achieve net-zero carbon without addressing operating theatres. The aim of this study was to prioritize feasible interventions to reduce the environmental impact of operating theatres. Methods This study adopted a four-phase Delphi consensus co-prioritization methodology. In phase 1, a systematic review of published interventions and global consultation of perioperative healthcare professionals were used to longlist interventions. In phase 2, iterative thematic analysis consolidated comparable interventions into a shortlist. In phase 3, the shortlist was co-prioritized based on patient and clinician views on acceptability, feasibility, and safety. In phase 4, ranked lists of interventions were presented by their relevance to high-income countries and low–middle-income countries. Results In phase 1, 43 interventions were identified, which had low uptake in practice according to 3042 professionals globally. In phase 2, a shortlist of 15 intervention domains was generated. In phase 3, interventions were deemed acceptable for more than 90 per cent of patients except for reducing general anaesthesia (84 per cent) and re-sterilization of ‘single-use’ consumables (86 per cent). In phase 4, the top three shortlisted interventions for high-income countries were: introducing recycling; reducing use of anaesthetic gases; and appropriate clinical waste processing. In phase 4, the top three shortlisted interventions for low–middle-income countries were: introducing reusable surgical devices; reducing use of consumables; and reducing the use of general anaesthesia. Conclusion This is a step toward environmentally sustainable operating environments with actionable interventions applicable to both high– and low–middle–income countries

Inhibitory Activity of Angiotensin 1-Converting Enzyme of Phosphopeptides Obtained from Proteolytic Hydrolyzates of Oyster, Crassostrea gigas

In the previous papers^(1.2), we investigated the effects of ACE inhibitory activities of phosphopeptides of P-1 and C-2 which were obtained from edible oyster by proteolytic hydrolyzation. In this investigation, the ACE inhibitory phosphopeptides of T-1 was further purified by ultrafiltration and Sephadex G-15 column chromatography. ACE inhibitory activity was fractionated into three major phosphopeptides fractions of T-1-1,T-1-2 and T-1-3 in the pepsin hydrolyzates of the T-1 by gel filtration rechromatography on Sephadex G-15. The inhibition of ACE of the three kinds of phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) was analyzed in vitro. The IC_ values of T-1-1,T-1-2 and T-1-3 of phosphopeptides for ACE were 0.159,0.095 and 0.140 mg protein/ml, respectively. The T-1-2 fraction had the most potent inyhibitory activity and showed 0.095 mg protein/ml inhibition against ACE at IC_ value. It has been demonstrated that the T-1-1,T-1-2 and T-1-3 contained about 33.3%, 3.01% and 27.12% as phosphonate-phosphorus of total phosphorus. The amino acid compositions of the phosphopeptides fractions (T-1-1,T-1-2 and T-1-3) were characterized by relatively high percentage for Tyr, Ser, Arg, Ala, Asp and Phe. When the ACE inhibitory phosphopeptides were analyzed by thin layer chromatography, some ninhydrine-positive spots were observed. These results suggest that the phosphopeptides are a mixture of several phosphopeptides

TYK2 Promoter Variant and Diabetes Mellitus in the Japanese

Background: Recently, natural mutation of Tyrosine kinase 2 (Tyk2) gene has been shown to determine susceptibility to murine virus-induced diabetes. In addition, a previous human genome-wide study suggested the type 1 diabetes (T1D) susceptibility region to be 19p13, where the human TYK2 gene is located (19p13.2). Methods: Polymorphisms of TYK2 gene at the promoter region and exons were studied among 331 healthy controls, and 302 patients with T1D and 314 with type 2 diabetes (T2D) in the Japanese. Findings: A TYK2 promoter haplotype with multiple genetic polymorphisms, which are in complete linkage disequilibrium, named TYK2 promoter variant, presenting decreased promoter activity, is associated with an increased risk of not only T1D (odds ratio (OR), 2.4; 95% confidence interval (CI), 1.2 to 4.6; P = 0.01), but also T2D (OR, 2.1; 95% CI, 1.1 to 4.1; P = 0.03). The risk is high in patients with T1D associated with flu-like syndrome at diabetes onset and also those without anti-glutamic acid decarboxylase autoantibody. Interpretation: The TYK2 promoter variant is associated with an overall risk for diabetes, serving a good candidate as a virus-induced diabetes susceptibility gene in humans. Funding: Ministry of Education, Culture, Sports, Science and Technology and of Health, Labor and Welfare of Japan