Está en la página 1de 3

Journal of Medicinal Plants Research Vol. 5(19), pp. 4974-4976, 23 September, 2011 Available online at http://www.academicjournals.

org/JMPR ISSN 1996-0875 2011 Academic Journals

Full Length Research Paper

Comparative study of similarity and identity of human albumin with some selected organism albumin
M. Akram1*, S. M. Ali Shah2, H. M. Asif2, Ghazala Shaheen2, Tahira Shamim2, M. Ibrahim Khan1, Asmat Ullah1 and Khalil Ahmed2
2

Shifa ul Mulk Memorial Hospital, Hamdard University, Karachi, Pakistan. College of Conventional Medicine, Islamia University, Bahawalpur, Pakistan.
Accepted 1 April, 2011

Alignment of protein sequences plays an important role in understanding the evolution of the protein. Albumin is a water soluble protein and is synthesized in liver in human. It is coagulated by heat and has carrier function in the body. In present study, albumin sequence was compared with rat, pig, cat and bovine albumin. On conclusion, it was found that that human albumin has highest similarity with cat albumin and lowest similarity with pig albumin. Human albumin has highest identity with cat albumin and lowest identity with pig albumin. Key words: Albumin, sequence alignment, comparative study. INTRODUCTION Sequence-alignment techniques have crucial role in modern molecular biology. Alignment methods may be used to search sequence databases for potential homologues. There are many programs to generate a multiple sequence alignment that identifies structurally and functionally important residues (Thompson, 1999; Waterman et al., 1978). There exist different programs like pair-wise and multiple sequence alignment (Robinson et al., 1981). In this article, the European molecular biology software suit (EMBOSS) has been used for pairwise alignment of protein. EMBOSS is an integral part in many analysis tasks that are usually designed to solve problems in comparative genomics, structure and function prediction, and homology modeling. Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca2+, Na+, K+, fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. It exerts oncotic pressure in the plasma. Deficiency of albumin results in the loss of carrier functions, and decreased oncotic pressure results in edema (Sding, 2005; Bao et al., 2001). SEQUENCE ALIGNMENT Sequence alignment is the procedure of comparing two (Pair-wise alignment) or more (multiple sequence alignment) sequenced by searching for a series of individual character or character patterns that are in the same order in the sequence (Anna et al., 2008; Katoh, 2002). There are two types of alignment, global alignment and local alignment. In global alignment entire sequence is aligned, using as many characters as possible, upto both ends of each sequence (Griffin et al., 1993; McClure, 1994; Briffeuil, 1998). Sequence that are quite similar and approximately the same length are suitable candidates for global alignment (Cheng et al., 1994; Riley et al., 1990; Sambrook et al., 1989; Rosenthal et al., 1990). In local alignment, stretches of sequence with the highest density of matches are aligned, thus generating one or more islands of matches or subalignment in the aligned sequences (Henikoff et al., 1997). Local alignments are more suitable for aligning sequences that are similar along some of their length, or sequences that share conserved region or domain (Harison, 2005; Victoria et al., 2007; Higgins et al., 1994). Sequence alignments unambiguously distinguish between protein pairs of similar and non-similar structure when the pairwise sequence identity is high (NotreDame et al., 2000; Edgar, 2004; NotreDame et al., 1996).

*Corresponding author. E-mail: makram_0451@hotmail.com. Tel: 92-021-6440083. Fax: 92-021-6440079.

Akram et al.

4975

Table 1. Sequence similarity and identity in human albumin and bovine albumin.

RESULTS AND DISCUSSION Previously, comparative study of lungfish albumin with tetrapod albumin and other fishes was done. Sequencing of lungfish generated 101 amino acids and had shown a high degree of identity with tetrapod albumins. Lungfish albumin has characteristics more akin with tetrapod albumin and less like those of other fish (Victoria et al., 2007). Present study does not provide any conclusive evidence about the relationships of rat with human, it does importantly, give some additional support for a closer relationship of rat album to human albumin, rather than to bovine, pig. The sequence alignment of albumin from different organisms and subsequent analysis may be a first step to revealing the true relationships. One of the most central methods in bioinformatics is the alignment of two protein or DNA sequences. Multiple sequence alignment gives insight into evolutionary, structural and functional relationships among the proteins. Here, a pair-wise sequence alignment has been used to determine the similarity and identity between Proteins. In the present study, Sequence similarity and identity in human albumin and bovine albumin has been found to be 536/609 (88.0%) and 465/609 (76.4%) respectively. Sequence similarity and identity in human albumin and cat albumin has been found to be 552/609 (90.6%) and 500/609 (82.1%) respectively. Sequence similarity and identity in human albumin and pig albumin has been found to be 462/609 (75.9%) and 462/609 (75.9%) respectively. Sequence similarity and identity in human albumin and rat albumin has been found to be 532/609 (87.4%) and 446/609 (73.2%) respectively. Conclusion Protein sequence alignment plays an important role in computational biology. In conclusion, it has been found that human albumin has highest similarity with cat albumin that is 90.6% and lowest similarity with pig albumin that is 75.9%. Like wise human albumin has highest identity with cat albumin that is 82.1% and lowest identity with pig albumin that is 73.2%.
REFERENCES

Similarity Identity

536/609 (88.0%) 465/609 (76.4%)

Table 2. Sequence similarity and identity in human albumin and cat albumin.

Similarity Identity

552/609 (90.6%) 500/609 (82.1%)

Table 3. Sequence similarity and identity in human albumin and pig albumin.

Similarity Identity

462/609 (75.9%) 462/609 (75.9%)

Table 4. Sequence similarity and identity in human albumin and rat albumin.

Similarity Identity

532/609 (87.4%) 446/609 (73.2%)

EMBOSS EMBOSS is European molecular biology open software suite. It is a free open source software analysis package. It is developed for the needs of the molecular biology user community. EMBOSS suite is available online. European molecular biology open software suite (EMBOSS) is a program suite for nucleic acid and protein sequence analysis. There are approximately 100 programs within EMBOSS. It is usually used for sequence alignment, rapid database searching with sequence patterns, domain analysis, Nucleotide sequence pattern analysis and Rapid identification of sequence patterns in large scale sequence sets (Walle, 2004; Morgenstern, 1999).
METHODOLOGY Sequence alignment is a tool in bioinformatics that is used to find homological relationships in large molecular databases. Sequences of human serum albumin, bovine albumin, pig albumin, rat albumin and cat albumin were searched in uniprotKB. These sequences were analyzed by using European molecular biology open soft ware suit (EMBOSS). Similarity and identity in sequences was recorded. Comparative study The comparative study is illustrated in Tables 1, 2, 3 and 4.

Chua ACN, Hsiao ESL, Yang YC, Lin LJ, Chou WM, Jason TC (2008). Gene Families Encoding 11S Globulin and 2S Albumin Isoforms of Jelly Fig (Ficus awkeotsang) Achenes. Biosci. Biotechnol. Biochem., 72: 506-513. Bao WG, Fukuhara H (2001). Secretion of human proteins from yeast: stimulation by duplication of polyubiquitin and protein disulfide isomerase genes in Kluyveromyces lactis . Gene, 272: 103-110. Briffeuil P (1998). Comparative analysis of multiple protein sequence alignment servers: Clues to enhance reliability of predictions. Bioinformatics, 14: 357-366. Cheng S, Chang SC, Gravitt P (1994). Independent evolution of the specialized pharyngeal jaw apparatus in cichlid and labrid fishes Respess R. Nat., 369: 684-685. Edgar RC (2004). MUSCLE: Multiple sequence alignment with high

4976

J. Med. Plant. Res.

accuracy and high throughput. Nucleic Acids Res., 32: 17921797. Griffin HG, Grifin AM (1993). DNA sequencing protocols. NJ: Humana Press. Harison S (2005). Sequence alignment and database searching, Fundamentals of Bioinformatics, I.K. International Publishing House, New Delhi, India, pp. 55-83. Henikoff S, Henikoff JG (1997). Embedding strategies for effective use of information from multiple sequence alignments. Protein Sci., 6: 698-705. Higgins D, Thompson J, Gibson T, Thompson JD, Higgins DG, Gibson TJ (1994). CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting,positionspecific gap penalties and weight matrix choice. Nucleic Acids Res., 22: 4673-4680. Katoh K (2002). MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier Transform. Nucleic Acids Res., 30: 3059-3066. McClure MA (1994). Comparative analysis of multiple protein sequence alignment methods. Mol. Biol. Evol., 11: 571-592. Morgenstern B (1999). DIALIGN2: Improvement of the segment-tosegment approach to multiple sequence alignment. Bioinformatics, 15: 211-218. NotreDame C, Coffee T (2000). A novel method for multiple sequence alignments. J. Mol. Biol., 302: 205-217. NotreDame C, Higgins DG (1996). SAGA: sequence alignment by genetic algorithm. Nucleic Acids Res., 24: 1515-1524.

Riley J, Butler R, Ogilivie D, Finniear R, Jenner D, Powell S, Anand R, Smith JC, Markham AF (1990). Nucleic Acids Res., 18: 2887-2890. Robinson DF, Foulds LR (1981). Comparison of phylogenetic trees. Math. Biosci., 53: 131-147. Rosenthal A, Jones DS (1990). Nucleic Acids Res., 18: 3095-3096. Sambrook J, Fritsch EF, Maniatis T (1989). Molecular Cloning: A Laboratory Manual. 2nd Edition. Cold Spring Harbor, NY.: Cold Spring Harbor Laboratory Press. Sding J (2005). "Protein homology detection by HMM-HMM comparison." Bioinformatics, 21(7): 951-960. Thompson JD (1999). BAliBASE: A benchmark alignment database for the evaluation of multiple alignment programs. Bioinformatics, 15: 8788. Victoria J, Peter M, Stephen O (2007). Comparative Biochemistry and Physiology Part B: Biochem. Mol. Biol., 147(3): 428-437. Walle V (2004). Align-mA new algorithm for multiple alignment of high divergent sequences. Bioinformatics, 20: 1428-1435. Waterman MS, Smith TF (1978). On the similarity of dendrograms. J. Theor. Biol., 73: 789-800.

También podría gustarte