Research Perspective on Biological Science Vol. 12

Unveiling the Therapeutic Potential of Cochlospermum tinctorium A Rich. (Bixaceae): A Biochemical Study

Sat, 06 Jun 2026 00:00:00 +0000

Cochlospermum tinctorium A. Rich. (Bixaceae) is a widespread herbaceous plant in the African Sahelian and Sudanian zones. Its root is used as a food and medicinal plant. This research aimed to use the C. tinctorium root as an efficient medicinal vegetable organ. The factors of hepatic diseases are multiple, and developing a single agent capable of preventing hepatic diseases at all times appears elusive. Finding a potent drug that can regenerate hepatic functions irrespective of the initial cause of the damage appears more feasible by using C. tinctorium. Studies of parameters were realised according to standard laboratory methods. At a threshold of \(\alpha\) = 0.05, significant correlations (p < 0.05) were found between secondary metabolite contents and functional activities such as radical scavenging activity of antioxidant component or hydroxyl radical scavenging activity. The value of DPPHH (1,1-diphenyl-2-picryl-hydrazyl) was 95.56 ± 0.94% for Cochlospermum tinctorium (CT) inner Matrix, with a variation of 0.12% for CT Soaked inner Matrix and 1.63% for CT Peeler. But Hydroxyl Radical Scavenging Activity (HRSA) was 37.14 ± 5.71 for CT inner Matrix, with a variation of -38.46% for CT Soaked inner Matrix and -71.79% for CT Peeler. Free radicals and other reactive species are thought to play an important role in many human diseases. Radical scavenging activities are very important due to the deleterious role of free radicals in biological systems. Cochlospermum tinctorium root has exhibited efficiency in healing many diseases thanks to multiple bioactive compounds. In addition, the colour of powders depended on chemical compounds. Finally, Cochlospermum tinctorium root was found to neutralise organic radicals and reactive oxygen species. The ability of C. tinctorium root extract to give hydrogen to neutralise free radicals enhances its application in multiple ways, such as treatments of hepatitis or in biochemical reactions, i.e., chelating of free radicals. Meanwhile, further investigations are necessary to facilitate the usage of the C. tinctorium, even combined with other medicinal vegetables.

Portable Point-of-Care Device for Simultaneous Quantification of G6PD Activity and Haemoglobin in Resource-Limited Settings

Sat, 06 Jun 2026 00:00:00 +0000

Glucose-6-phosphate dehydrogenase deficiency is one of the most prevalent enzymatic disorders worldwide. It carries significant clinical implications, particularly in the management of neonatal hyperbilirubinemia and the safe administration of oxidative medications in malaria-endemic regions. Accurate and timely detection of G6PD deficiency is therefore essential to minimise the risk of severe, potentially life-threatening hemolytic crises, thereby improving patient safety and clinical outcomes.

This study evaluates the MyG6PD device, a novel quantitative point-of-care (PoC) diagnostic tool that simultaneously assesses haemoglobin concentration and G6PD enzyme activity. The analytical performance of the device was benchmarked against gold-standard laboratory spectrophotometry and the commercially available STANDARD G6PD Analyzer™. MyG6PD exhibited exceptional Linearity (R2 ≥ 0.99), high accuracy (bias < ±15%), and robust precision (CV < 15%) across deficient, intermediate, and normal activity ranges. Crucially, it successfully identified heterozygous females presenting with intermediate phenotypes. MyG6PD demonstrated greater precision and reproducibility in detecting intermediate G6PD phenotypes than the SD Biosensor, enabling clear differentiation between normal and mosaic expression. Furthermore, its lower manufacturing and per-test costs inherently enhance its scalability for global health initiatives. Characterised by a compact, battery-operated architecture, rapid turnaround times, and minimal training requirements, the device is uniquely suited for decentralised, resource-limited environments. Its cost-effective consumables and reliable detection of intermediate G6PD activity underscore its immense potential for large-scale clinical deployment. Ultimately, MyG6PD delivers an accessible, reliable, and clinically actionable screening solution that enables the safer administration of oxidative therapies and improves patient outcomes in high-risk demographic zones. Capable of reliably identifying deficient and intermediate Glucose-6-phosphate dehydrogenase deficiency phenotypes, MyG6PD represents a highly feasible and cost-effective intervention to support the safe administration of oxidative therapies and reduce the risk of hemolytic crises among vulnerable populations in resource-limited settings.

Purification and Physicochemical Characterisation of Glycolate Oxidase from Pea (Pisum sativum L.) and Sorghum (Sorghum sudanense) via Ion-Exchange Chromatography

Saba Hadi, Zahraa B. Mohammed, Sara H. Oubid, Majid A. AL-Bayati — Sat, 06 Jun 2026 00:00:00 +0000

The glycolate oxidase enzyme, a core photorespiratory enzyme in green plants, oxidises glycolate to glyoxylate, playing an adaptive role in roots during hypoxia to normoxia transition. Despite increasing interest in the physiological significance of these enzymes, comparative biochemical characterisation of Lactate oxidase-like (LCO) glycolate oxidase from agronomically important species remains limited. The present study aimed to purify glycolate oxidase enzymes from peas (Pisum sativum L.) and sorghum (Sorghum sudanense J.), and investigate their physicochemical and regulatory properties. The activity of one of the glycolate oxidase isoforms (LCO-like glycolate oxidase) was induced in pea and sorghum leaves. The enzymes were purified to an electrophoretically homogeneous condition. The purified enzymes' specific activity, molecular mass, and physicochemical characteristics were determined. Electrophoretically homogeneous LCO-like glycolate oxidase preparations were successfully obtained from both plant species. The results showed that the LCO-like glycolate oxidase enzyme from pea leaves was 314.37E/mg proteins, the degree of purification was 207 times, and the yield was 11.5%. The sorghum leaf enzyme was 274.22E/mg proteins with the degree of purification and yield, estimated at 143 times and 13.8%, respectively. The molecular mass of the native enzymes was 182 and 168kDa for peas and sorghum, respectively. It was revealed that the enzyme consisted of four subunits with a molecular mass of 45 and 42kDa for glycolate oxidase from pea and sorghum leaves, respectively, indicating a homo-tetramer. The sorghum leaf enzyme exhibited a higher affinity for lactate substrate with an optimal temperature of 55°С and pH of 7.2. Meanwhile, the optimal temperature and pH of pea leaf enzyme were 50°C and 7.5, respectively. The study successfully established a multistep purification strategy for obtaining homogeneous LCO-like glycolate oxidase enzymes from pea and sorghum leaves. The availability of homogeneous specimens provides opportunities to investigate the role of LCO-like glycolate oxidase in the adaptive reactions of cellular plant metabolism.