Philippine Journal of Science
151 (1): 275-280, February 2022
ISSN 0031 – 7683
Date Received: 21 July 2021

[RESEARCH NOTE]

Molecular Characterization and Polymorphism
of Inhibin (INHβA) Gene in Water Buffalo
(Bubalus bubalis) Bulls

Sanny C. Babera, Mary Rose D. Uy, Gabriel Alexis SP. Tubalinal,
Felomino V. Mamuad, and Claro N. Mingala

¹College of Animal Science and Veterinary Medicine
President Ramon Magsaysay State University–San Marcelino Campus
San Marcelino, Zambales, Philippines
²Department of Animal Science, College of Agriculture
Central Luzon State University, Science City of Muñoz
3120 Nueva Ecija, Philippines
³Philippine Carabao Center, Maharlika Highway
Science City of Munoz 3120, Nueva Ecija, Philippines

Corresponding author: cnmingala@clsu.edu.ph
Both authors contributed equally to this work

 

[Download]
Babera S et al. 2022. Molecular Characterization and Polymorphism of Inhibin (INHβA) Gene in
Water Buffalo (Bubalus bubalis) Bulls. Philipp J Sci 151(1): 275–280. https://doi.org/10.56899/151.01.20

 

ABSTRACT

The study characterized inhibin-βA (INHβA) gene of 12 water buffalo (Bubalus bubalis) bulls [two Philippine Carabao (PC), five Bulgarian Murrah (BM), and five Italian Murrah (IM)] using DNA extracted from semen. Using MEGA 7.0 software and Signal P® version 4, the sequences were assembled and aligned and amino acid sequences were determined, respectively. BM bull sequence showed 100% similarity with B. bubalis from the National Center for Biotechnology Information (NCBI) database. However, a lower similarity was seen on both PC and IM at 98%. The translated amino acid sequence of PC, BM, and IM had 95, 97, and 93% similarity with B. bubalis sequence from NCBI, respectively. The phylogeny tree revealed that both PC and IM were closely similar in their gene sequence, while BM was more similar with B. bubalis from NCBI. Their similarities in nucleotide sequence suggest that INHβA gene was conserved in bulls. The signal peptide was observed in BM and B. bubalis from NCBI. BM has an amino acid exchanged from threonine to alanine, while in B. bubalis has an amino acid exchanged from histidine to aspartic acid. This polymorphism from their cleaving site could cause an interaction in the reproduction, growth, and maintenance of the bull.