Locally Adaptive Block Thresholding Method with Continuity Constraint

We present an algorithm that enables one to perform locally adaptive block thresholding, while maintaining image continuity. Images are divided into sub-images based some standard image attributes and thresholding technique is employed over the sub-images. The present algorithm makes use of the thresholds of neighboring sub-images to calculate a range of values. The image continuity is taken care by choosing the threshold of the sub-image under consideration to lie within the above range. After examining the average range values for various sub-image sizes of a variety of images, it was found that the range of acceptable threshold values is substantially high, justifying our assumption of exploiting the freedom of range for bringing out local details.Comment: 12 Pages, 4 figures, 1 Tabl

Urinary tract infection caused by Myroides spp. in diabetic patients: To be or not to be

Myroides is a non-fermentative, Gram-negative rod-like bacteria. It is a rare opportunistic pathogen which has been reported to cause many serious infections. Management of infections caused by Myroides can be challenging due to its high resistance to most antibiotics. We report three cases of urinary tract infection (UTI) due to Myroides species in patients with diabetes mellitus Type II. Myroides spp. isolated were resistant to all the antibiotics tested: Amoxicillin-clavulanic acid, piperacillin-tazobactam, cefepime, ceftriaxone-cefoperazone sulbactam, amikacin, gentamicin, imipenem, meropenem, ciprofloxacin, colistin, tigecycline, and co-trimoxazole. Two strains were sensitive to minocycline (minimum inhibitory concentration <1 μg/mL). Two patients had Foley’s catheter in place and one patient had urinary retention at the time of diagnosis. The infection in two cases was nosocomial, whereas one case appeared to have a community-acquired infection with Myroides. Clinicians should consider the possibility of Myroides as a pathogen in UTI in diabetic patients, especially in nosocomial settings

Functional Insight into the C-Terminal Extension of Halolysin SptA from Haloarchaeon Natrinema sp. J7

Halolysin SptA from haloarchaeon Natrinema sp. J7 consists of a subtilisin-like catalytic domain and a C-terminal extension (CTE) containing two cysteine residues. In this report, we have investigated the function of the CTE using recombinant enzymes expressed in Haloferax volcanii WFD11. Deletion of the CTE greatly reduced but did not abolish protease activity, which suggests that the CTE is not essential for enzyme folding. Mutational analysis suggests that residues Cys303 and Cys338 within the CTE form a disulfide bond that make this domain resistant to autocleavage and proteolysis under hypotonic conditions. Characterization of full-length and CTE-truncation enzymes indicates the CTE not only confers extra stability to the enzyme but also assists enzyme activity on protein substrates by facilitating binding at high salinities. Interestingly, homology modeling of the CTE yields a β-jelly roll-like structure similar to those seen in Claudin-binding domain of Clostridium perfringens enterotoxin (clostridial C-CPE) and collagen binding domain (CBD), and the CTE also possesses collagen-binding activity, making it a potential candidate as an anchoring unit in drug delivery systems

Two step purification of acinetobacter sp. Lipase and its evaluation as a detergent additive at low temperatures

10.1007/s12010-008-8143-1Applied Biochemistry and Biotechnology1502139-15