Article3 Biotech2024
Agricultural wastes: a new promising source for phenylalanine ammonia-lyase as anticancer agent.
Article in 3 Biotech, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Genome-wide analysis and expression profiling of the phenylalanine ammonia-lyase gene family in Chrysanthemum morifolium.BMC plant biology · 2026Article
- Phenylalanine Ammonia-Lyase: A Core Regulator of Plant Carbon Metabolic Flux Redistribution-From Molecular Mechanisms and Growth Modulation to Stress Adaptability.Plants (Basel, Switzerland) · 2025Review
- Enhancing the Stability and Anticancer Activity ofPolymers · 2024Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The present study aims to investigate the physicochemical characteristics of phenylalanine ammonia-lyase (PAL) extracted from agricultural waste and its potential use as an anticancer agent in comparison to microbial PAL. We extracted and partially purified PAL from agricultural waste sources. We assessed the temperature and pH range of PAL and determined enzyme kinetics parameters including Michaelis constants (Km), maximum velocity (Vmax), and specificity constant values (Vmax/Km). Additionally, we examined the effects of different storage temperatures on PAL activity. In our analysis, we compared the efficacy of agricultural waste-derived PAL with PAL from
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Registered trials
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