Hatem Hassan Abd-Elrahman
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Hatem Hassan Abd-Elrahman has a total of 4 co-authors. Here are the top co-authors by number of shared publications:
- Hazem Abdallah Elnashar
Giza Memorial Institute for Ophthalmic Research (MIOR), Giza, Egypt
1 shared publication Mahmod M. Omran
School of Biotechnology, Nile University, Giza, Egypt
1 shared publicationWael A. Omar
Biology Department, College of Science, Taif University, Taif, Kingdom of Saudi Arabia
1 shared publication- Wael Abdel-Moneim Omar
Department of Biology, College of Science, Taif University, Taif, Saudi Arabia
1 shared publication
Latest Publications
- 23 September 2026
- Published by Springer Nature in Environmental Biology of Fishes
- Vol. 109 (4) , 146
Combined approach of dose–response modeling and biomarker analysis during acute barium toxicity of Nile tilapia, Oreochromis niloticus
- 23 September 2026
- Published by Springer Nature in Environmental Biology of Fishes
- Vol. 109 (4) , 146
Combined approach of dose–response modeling and biomarker analysis during acute barium toxicity of Nile tilapia, Oreochromis niloticus
- Open Access
- 13 March 2024
- Published by Springer Nature in Future Journal of Pharmaceutical Sciences
- Vol. 10 (1) , 1-8
Characterization of biochemical and optical properties of Nile tilapia (Oreochromis niloticus) corneal collagen
Background: Collagen extracted from fish body parts is a promising biological material. It has an important role in many pharmaceutical, medical applications and tissue engineering such as corneal regeneration and stromal replacement. The present work investigates a new trend to extract collagen from the fish cornea, as a prospected substituent of human corneal collagen by characterizing some biochemical and optical properties of the fish corneal collagen. Results: Examination of the corneal tissue of Nile tilapia; Oreochromis niloticus was conducted using electron microscopy, Fourier transform infrared (FTIR) spectroscopy, UV–visible spectrophotometry, optical properties, and thermal properties. The fish were divided into 10 groups each of which consisted of 5 fish. 2 groups of fish were examined for each technique. Results indicated that the corneal layers of O. niloticus are thin at the center and thicker at the periphery with the stroma consisting of a triple helical structure collagen type I. The fish cornea showed very weak transmission at the UV regions (190 nm) and maximum transmission at the visible regions. The values of transmission (T), reflected light (R) and scattered light (S) were 2.685 mw, 100 × 10−3 mw at 45° and 40 × 10−3 mw, respectively. Consequently, the percentage of absorbed light is 21.76%. The denaturation temperature of the fish corneal stroma is 22.27 °C. Conclusions: The method for obtaining fish collagen affects the specific properties of collagen and consequently its further uses as a potential biomedical substituent for mammalian collagen. Specification of the fish species and tissue type is crucial in identifying the quality as well as the physical and functional properties of the extracted collagen.
- 13 March 2024
- Published by Springer Nature in Future Journal of Pharmaceutical Sciences
- Vol. 10 (1) , 1-8
Open AccessCharacterization of biochemical and optical properties of Nile tilapia (Oreochromis niloticus) corneal collagen
Background: Collagen extracted from fish body parts is a promising biological material. It has an important role in many pharmaceutical, medical applications and tissue engineering such as corneal regeneration and stromal replacement. The present work investigates a new trend to extract collagen from the fish cornea, as a prospected substituent of human corneal collagen by characterizing some biochemical and optical properties of the fish corneal collagen. Results: Examination of the corneal tissue of Nile tilapia; Oreochromis niloticus was conducted using electron microscopy, Fourier transform infrared (FTIR) spectroscopy, UV–visible spectrophotometry, optical properties, and thermal properties. The fish were divided into 10 groups each of which consisted of 5 fish. 2 groups of fish were examined for each technique. Results indicated that the corneal layers of O. niloticus are thin at the center and thicker at the periphery with the stroma consisting of a triple helical structure collagen type I. The fish cornea showed very weak transmission at the UV regions (190 nm) and maximum transmission at the visible regions. The values of transmission (T), reflected light (R) and scattered light (S) were 2.685 mw, 100 × 10−3 mw at 45° and 40 × 10−3 mw, respectively. Consequently, the percentage of absorbed light is 21.76%. The denaturation temperature of the fish corneal stroma is 22.27 °C. Conclusions: The method for obtaining fish collagen affects the specific properties of collagen and consequently its further uses as a potential biomedical substituent for mammalian collagen. Specification of the fish species and tissue type is crucial in identifying the quality as well as the physical and functional properties of the extracted collagen.