Preparation and partial characterization of amino acid transporting brush border membrane vesicles from the larval midgut of the cabbage butterfly (Pieris brassicae)

Objective— To determine whether serum γ-glutamyl transferase (GGT) predicts cardiovascular disease (CVD) morbidity and mortality, accounting for temporal changes in known CVD risk factors and C-reactive protein (CRP).

Methods and Results— In 3451 Framingham Study participants (mean age 44 years, 52% women) we examined the relations of GGT with CVD risk factors, and prospectively determined the risk of new-onset metabolic syndrome, incident CVD, and death. GGT was positively associated with body mass index, blood pressure, LDL cholesterol, triglycerides, and blood glucose in cross-sectional analysis ( P <0.005). On follow-up (mean 19 years), 968 participants developed metabolic syndrome, 535 developed incident CVD, and 362 died. The risk of metabolic syndrome increased with higher GGT (multivariable-adjusted hazard ratio [HR] per SD increment log-GGT, 1.26 [95%CI; 1.18 to 1.35]). Adjusting for established CVD risk factors (as time-dependent covariates updated quadriennially) and baseline CRP, a 1-SD increase in log-GGT conferred a 13% increase in CVD risk ( P =0.007) and 26% increased risk of death ( P <0.001). Individuals in the highest GGT quartile experienced a 67% increase in CVD incidence (multivariable-adjusted HR 1.67, 95%CI; 1.25 to 2.22).

Conclusion— An increase in serum GGT predicts onset of metabolic syndrome, incident CVD, and death suggesting that GGT is a marker of metabolic and cardiovascular risk.

Gamma glutamyl transferase and metabolic syndrome, cardiovascular disease, and mortality risk: the Framingham Heart Study.

The enzyme designated by the IUPAC Commission as EC.2.3.2.2 has been variously trivialized in the literature as γ-glutamyl transpeptidase, D-glutamyltransferase, and γ-glutamyltransferase. The latter (abbreviated as GGT) will be employed in this review.

Structural, functional, and clinical aspects of gamma-glutamyltransferase.

Intrabiliary glutathione hydrolysis. A source of glutamate in bile.

Publisher Summary This chapter focuses on the kinetics and mechanism of γ-glutamyl transpeptidase Three catalytic activities are associated with γ-glutamyl transpeptidase All of these activities involve the transfer of the γ-glutamyl moiety of glutathione (or of other γ-glutamyl compounds such as glutamine, glutathione disulfide, glutathione S-conjugates, and model substrates such as γ-glutamyl- p -nitroanilide) to an acceptor substrate Transpeptidation occurs when the acceptor is an amino acid, dipeptide, or tripeptide, leading to formation of the corresponding γ-glutamyl amino acid or γ-glutamyl dior tripeptide If an amino acid acceptor contains two stereochemically distinct α-aminogroups from which two separate γ-glutamyl products are formed, the experimentally determined kinetic parameters are composite values reflecting both activities L-Cystathionine is such a substrate for γ-glutamyl transpeptidase At L-γ-glutamyl donor concentrations less than 30 μ M , L-cystathionine exhibits a relative reactivity (V b /K b ) comparable to that of L-cystine, the most active acceptor of the common amino acids

gamma-Glutamyl transpeptidase: kinetics and mechanism.

We describe a method for measuring γ-glutamyltransferase (EC 2.3.2.2) activity in serum, which can be used with automated enzyme analyzers (such as the LKB 8600 Reaction Rate Analyzer) that require enzyme reactions to be initiated with substrate. The method also permits optimal determination conditions to be obtained at 37 °C. The enzymatic reaction is commenced by adding γ-glutamyl- p -nitroanilide dissolved in dilute hydrochloric acid to samples pre-incubated with tris(hydroxymethyl)aminomethane—glycylglycine buffer. The p -nitroaniline liberated is continously monitored at 37 °C at 405 nm. The pH of the pre-incubation buffer is such that the optimal pH for the enzyme reaction results from addition of the acid substrate solution.

Optimized Determination of γ-Glutamyltransferase by Reaction-Rate Analysis

Handle everyday research tasks with reliable, citation-backed results

Your personal Research Agent to handle research tasks with citation-backed results

Popular Tasks used by Researchers

How can I help with your research?

Meet SciSpace

Get more enhanced response by uploading the PDFs you want me to reference.

No relevant PDFs in your library

SciSpace is the AI research assistant for academics. Run systematic literature reviews on 280M+ papers, and write papers with cited sources. Trusted by 1M+ students, PhDs & researchers.

SciSpace | AI for Research

Analyze PDFs

Code & Manuscripts

Funding & Grants

Literature & Patents

Medical & Clinical Data

Systematic Review

Visualize & Present

Web & Data

Build a Google Scholar-like website for your research.

Build a website

Create charts and images for your research

Create a Chart

Write a paper for submission to a journal

Draft a manuscript

Patent Search

Design eye-catching scientific posters in minutes.

Scientific Poster Generation

Systematic Literature Review

One task is running at the moment. Your messages will be shown right after.

Drag and drop or click here to browse

Loved by <highlight>1 million+</highlight> researchers

Extract a list of specific topics and their sources from unstructured text

Topics

Compare and analyze relevant papers that matches with your search

Papers

Get insights from PDFs and bookmarked papers from your library

My library

Recent searches

Try searching for:

Catch AI-generated content in scholarly and non-scholarly content

{ai} Detector

Ai Writer

Get PDF Summaries, highlighted text explanations 

Chat with PDF

Effortlessly create in-text citations and bibliographies in APA and 2,500 other formats

Citation generator

Get explanations, summaries, and answers on academic papers

Ease up your research workflow with {scispace}'s cohort of exciting AI tools

Elevate your academic writing skills and convey your ideas the way you want

Paraphraser

Explore our range of reading and writing tools

Your file is being prepared and should be ready in a few minutes. If it's a large file, it might take a bit longer. You can close this window, and we'll email you the file when it's done.

You have reached a maximum limit of <strong>{limit}</strong> columns in the table. Remove at least <strong>1</strong> column to add or create another one.

David Tarlow

Author Tools

Chat about Author

Papers

Optimized Determination of γ-Glutamyltransferase by Reaction-Rate Analysis