Proteases are one of the highest value commercial enzymes as they have broad applications in food, pharmaceutical, detergent, and dairy industries and serve as vital tools in determination of structure of proteins and polypeptides. Multiple application of these enzymes stimulated interest to discover them with novel properties and considerable advancement of basic research into these enzymes. A broad understanding of the active site of the enzyme and of the mechanism of its inactivation is essential for delineating its structure-function relationship. Primary structure analysis of alkaline protease showed 42% of its content to be alpha helix making it stable for three dimensional structure modeling. Homology model of alkaline protease has been constructed using the X-ray structure (3F7O) as a template and swiss model as the workspace. The model was validated by ProSA, SAVES, PROCHECK, PROSAII and RMSD. The results showed the final refined model is reliable. It has 53% amino acid sequence identity with the template, 0.24 Å as RMSD and has -7.53 as Z-score, the Ramachandran plot analysis showed that conformations for 83.4 % of amino acid residues are within the most favored regions and only 0.4% in the disallowed regions.

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Background: There is a lacuna of information regarding the dimensions of the gluteal arteries. Aim: The present study is to present a detailed account of the pattern of blood supply dimensions of the superior and inferior gluteal arteries. Methods: 62 pelvic halves embalmed with a modified Larssen solution Results & Conclusion: Variations were observed in the origin, course, distribution, and dimensions of superior gluteal (6.45%) and inferior gluteal arteries (9.68%) which are significant, considering the importance of management of clinical conditions associated with the gluteal region like gluteal claudication, neuralgia, and harvesting of perforator flaps.

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