👤 J F Riordan

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2
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2
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Also published as: James Michael O Riordan
articles
David Sciascia, Paul Neary, Shaheel Sahebally +5 more · 2025 · Digestive surgery · added 2026-04-24
This study aims to investigate the current evidence regarding long-term outcomes using laparoscopic peritoneal lavage (LPL) versus primary bowel resection (PR) in Hinchey III diverticulitis. A systema Show more
This study aims to investigate the current evidence regarding long-term outcomes using laparoscopic peritoneal lavage (LPL) versus primary bowel resection (PR) in Hinchey III diverticulitis. A systematic review was undertaken based upon articles published between January 1, 2000, and March 1, 2024. Databases Pubmed, Scopus, and Embase were used employing the key search terms "Diverticulitis" and "Peritoneal Lavage." Articles were selected according to the PRISMA guidelines and statistical analysis was undertaken. Cumulative analysis of diverticulitis recurrence and secondary outcomes of disease-related mortality, serious adverse events, stoma incidence, reoperation, and readmission rates were performed. An initial search identified 506 articles for review. A total of 294 patients were included for final analysis from 3 prospective randomized controlled trials. There was no significant difference in disease-related mortality or serious adverse events between LPL and PR. There was significantly decreased likelihood of having a stoma in the LPL group; however, there was also a significantly increased likelihood of having recurrent diverticulitis. There was heterogenicity across all trials. There is a paucity of level 1 evidence available regarding the long-term outcomes of Hinchey III diverticulitis managed with LPL. At 3-year follow-up, there is a significantly decreased likelihood of having a stoma, tempered by the fact that there is a significantly increased likelihood of having recurrent diverticulitis. Further homogenous high-quality randomized studies are required to clarify whether LPL shows long-term benefit over PR. Show less
no PDF DOI: 10.1159/000543241
LPL
B M Solomon, K S Larsen, J F Riordan · 1990 · Biochemistry · ACS Publications · added 2026-04-24
Limited proteolysis of carboxypeptidase A from bovine pancreas with subtilisin Carlsberg generates a stable intermediate, carboxypeptidase S, whose esterase and peptidase activities are increased and Show more
Limited proteolysis of carboxypeptidase A from bovine pancreas with subtilisin Carlsberg generates a stable intermediate, carboxypeptidase S, whose esterase and peptidase activities are increased and decreased, respectively, under standard assay conditions. Carboxypeptidase S was isolated by affinity chromatography. Sequence analysis shows that it is cleaved solely at the Ala154-Gly155 bond. Its enzymatic properties were determined under stopped-flow conditions with Dns-Gly-Ala-Phe and its ester analogue Dns-Gly-Ala-OPhe. For both substrates, the Km values are increased 30-40-fold. The kcat value for peptide hydrolysis is virtually unaffected whereas that for ester hydrolysis is increased 10-fold. The magnitude of the Km effect is equivalent to a loss of 9 kJ/mol of binding energy and likely reflects a disruption of the network of hydrogen bonds that links Tyr-248 and Arg-145 to the backbone carbonyls of Ala-154 and Gly-155. The difference in kcat effects for the two substrate classes is related to differences in the chemical nature of the rate-determining step. Product release is rate determining for catalytic hydrolysis of ester substrates, and hence, the increase in kcat indicates that dissociation of products is facilitated as a result of the Ala154-Gly155 bond scission. The changes in enzymatic activity accompanying limited proteolysis are due to conformational alterations in the vicinity of the active center of the molecule. The affinity of a monoclonal antibody, mAb 100, directed toward the antigenic determinant located between residues 209 and 218 in carboxypeptidase A is diminished considerably for carboxypeptidase S.(ABSTRACT TRUNCATED AT 250 WORDS) Show less
no PDF DOI: 10.1021/bi00483a021
CPS1