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Annisa Nur Hasanah
Universitas Bakti Tunas Husada, Indonesia

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Development of a natural eosinophil stain based on cordyline fruticosa leaves extract and selenicereus monacanthus (dragon fruit peel extracts) for hematology diagnostic applications Annisa Nur Hasanah; Yane Liswanti; Meti Kusmiati; Aliya Fitria Salsabila; Linda Prihartini
Science Midwifery Vol 13 No 6 (2026): February: Health Sciences and related fields
Publisher : Institute of Computer Science (IOCS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35335/midwifery.v13i6.2268

Abstract

The search for natural alternatives to conventional hematological stains has gained attention due to issues of dependency on imported reagents, cost, and potential environmental impact. This study aimed to explore the potential of Cordyline fruticosa (andong leaves) and Selenicereus monacanthus (dragon fruit peel) extracts as natural eosinophil stains in hematology. Pigment extraction was performed using standard procedures, followed by phytochemical screening for anthocyanins and flavonoids. The total anthocyanin content was higher in C. fruticosa (1.20 mg/L) compared to S. monacanthus (0.30 mg/L), while relative flavonoid absorbance values also indicated greater pigment density in andong leaves. Application of the extracts in the hemocytometer method demonstrated staining of the background and cellular components, although with weaker intensity than conventional eosin. In peripheral blood smear preparations, Giemsa stain produced the most distinct results, clearly differentiating eosinophil nuclei, cytoplasm, and characteristic granules. In contrast, the natural extracts yielded paler orange cream staining, with less clarity and limited granule visualization, and some smears exhibited detachment due to imperfect fixation. These findings suggest that while andong leaves and dragon fruit peel contain bioactive pigments with staining potential, their application in hematology requires further optimization, particularly in fixation methods, extract concentration, and stability testing over longer storage periods. 
SDS-PAGE characterization of dialyzed protein fractions from mycobacterium tuberculosis isolates for tuberculosis biomarker screening Githa Agripina Barokah; Korry Novitriani; Annisa Nur Hasanah; Dina Ferdiani; Fransisca Probo Setyoningrum
Science Midwifery Vol 14 No 1 (2026): April: Health Sciences and related fields
Publisher : Institute of Computer Science (IOCS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35335/midwifery.v14i1.2333

Abstract

Tuberculosis is an infectious disease caused by Mycobacterium tuberculosis, in which the identification of protein profiles serves as an important approach in diagnostic research and specific antigen development. This study aimed to analyze the protein profile of dialyzed fractions from Mycobacterium tuberculosis isolates using the SDS-PAGE (Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis) method. Protein isolation was carried out through sonication at 4 °C to lyse the cells and release intracellular proteins without causing denaturation. The resulting lysate supernatant was subjected to 30% ammonium sulfate precipitation to separate proteins based on their solubility, followed by dialysis to remove residual salts and unwanted small molecules. The total protein concentration was measured using a photometer with a total protein reagent, showing a relatively low value, indicating that the protein fraction was concentrated on specific molecules with higher purity. The SDS-PAGE analysis revealed the presence of a protein band with an estimated molecular weight of 77,6 kDa, suggesting the successful purification of protein fractions based on molecular weight. Based on these findings, it can be concluded that the combination of sonication, ammonium sulfate precipitation, and dialysis is effective as a preliminary purification method to obtain purer proteins from Mycobacterium tuberculosis isolates and enables more specific characterization of protein profiles through SDS-PAGE.