Ganong's review of medical physiology , Ganong's review of medical physiology , کتابخانه دیجیتال جندی شاپور اهواز

Ganong's review of medical physiology

Neem (Azadirachta indica): An indian traditional panacea with modern molecular basis.

Type II diabetes mellitus (T2DM) is a fast-growing epidemic affecting people globally. Furthermore, multiple complications and comorbidities are associated with T2DM. Lifestyle modifications along with pharmacotherapy and patient education are the mainstay of therapy for patients afflicted with T2DM. Western medications are frequently associated with severe adverse drug reactions and high costs of treatment. Herbal medications have long been used in the treatment and prevention of T2DM in both traditional Chinese medicine (TCM) and traditional Indian medicine (TIM). This review examines in vivo, in vitro, and clinical evidence supporting the use of various herbs used in TCM and TIM. The problems, challenges, and opportunities for the incorporation of herbal frequently used in TCM and TIM into Western therapy are presented and discussed.

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Treating type 2 diabetes mellitus with traditional chinese and Indian medicinal herbs.

Targeting obesity with plant-derived pancreatic lipase inhibitors: A comprehensive review.

Neem (Azadirachta indica) and its Potential for Safeguarding Health of Animals and Humans: A Review

Azadirachta indica, used in antidiabetic herbal drugs, was reported to contain α-glucosidase inhibitor. Bioassay guided purification characterized the inhibitor as nimbidiol (a diterpenoid), present in root and stem-bark of the tree. Nimbidiol inhibited intestinal (mammalian) maltase-glucoamylase, sucrase-isomaltase, lactase, trehalase and fungal α-glucosidases. Nimbidiol showed a mixed competitive inhibition on intestinal carbohydrases. IC50, Ki and Ki' (µM) were 1.35 ± 0.12, 0.08 ± 0.01, 0.25 ± 0.11, respectively, for maltase-glucoamylase (maltotetraose as substrate). Nimbidiol was more potent inhibitor of isomaltase (IC50 0.85 ± 0.035 µM), lactase (IC50 20 ± 1.33 µM) and trehalase (IC50 30 ± 1.75 µM) than acarbose, voglibose, salacinol, kotalanol and mangiferin. Ki and Ki' values (µM) for intestinal sucrase were 0.7 ± 0.12 and 1.44 ± 0.65, respectively. Development of nimbidiol as an antidiabetic drug appears to be promising because of broad inhibition spectrum of intestinal glucosidases and easy synthesis of the molecule.

https://www.tandfonline.com/doi/pdf/10.3109/14756366.2012.694877

Characterization of nimbidiol as a potent intestinal disaccharidase and glucoamylase inhibitor present in Azadirachta indica (neem) useful for the treatment of diabetes

Dietary excess of lipids causes substantial health disorders like hyperlipemia, obesity and cardiovascular problems. Use of lipase and α-glucosidase inhibitors in combination is considered to be the ideal therapy for obesity control. Anti-obesity activity of natural products is usually assessed by inhibition of pancreatic lipase activity by the preparations. We have reported earlier that some known hypoglycemic medicinal plants, such as, Eugenia jambolana Lam., Azadirachta indica A. Juss., Tinospora cordifolia (Thunb.) Miers and Trigonella foenum-graceum L. contain α-glucosidase inhibitors. The present study reports that their plant extracts also inhibit pancreatic lipase activity. The methanolic extracts showed an IC50 value (μg/mL) of 230+20, 520+15, 360+25 and 564+12 for E. jambolana (stem-bark), A. indica (root), T. cordifolia (leaves) and T. foenum-graceum (seeds), respectively. Bioassay guided partial purification yielded active fractions with IC50 (μg/mL) of 23+5 (E. jambolana), 14+3 (A. indica) and 11+2.5 (T. cordifolia). All the active fractions inhibited the enzyme in a mixed-competitive manner with Ki and Ki’ values (μg/mL) as 1.26+0.22, 3.96+0.28 (E. jambolana); 0.95+0.46, 2.3+0.16 (A. indica); and 1.1+0.2, 4.2+0.26 (T. cordifolia).

/pdf/indian-medicinal-plants-known-to-contain-intestinal-5203ddi8ha.pdf

Indian medicinal plants known to contain intestinal glucosidase inhibitors also inhibit pancreatic lipase activity—An ideal situation for obesity control by herbal drugs

It is a global need to realize noninvasive, simple, rapid, selective, inexpensive, and portable assessment methods for diagnosis of diseases. Enzyme-based bio-sensing system, compared with traditional analytical methods, has all such potential attributes. This paper proposes carbonic anhydrase enzyme (CA) (E.C. 4.2.1.1)-based cost-effective, highly selective, and reproducible CO2 biosensing system that can measure CO2 concentration (ppm level) in expired breath accurately to give valuable information for assessing the respiratory disorders of the subjects. CA is extracted from spinach leaves and immobilized on an electrode assembly. The assembly generates a sensible electrical signal (mV) when brought in contact with the aqueous CO2. The sensor characterizes a linear response from 160–2677 ppm of CO2 concentration dissolved in water, good sensitivity (~0.132mV/ppm) with excellent fast response time within 12s. The features include repeatability, shelf life (~5 months), re-usability (~20 times), and selective responsiveness to the CO2 molecules in the exhaled breath. The feasibility for the use of the biosensor in a suitable setup for home-based monitoring of CO2 in exhaled breath has been proposed and justified. The device showed a good correlation between the results obtained from the sensor and established clinical test.

Development and Characterization of Carbonic Anhydrase-Based CO 2 Biosensor for Primary Diagnosis of Respiratory Health

Production of acetyl esterase by Termitomyces clypeatus was stimulated by xylan, cellulose, arabinose and arabinose-containing polysaccharides in the growth medium. The culture filtrate was equally active with p-nitrophenyl acetate and acetyl xylan. Acetyl xylan was completely deacetylated by the enzyme. Activity was optimum at pH 6.5 and at 50iC. The Km values for p-nitrophenyl acetate and acetyl xylan were 0.83 mM and 0.38% (w/v) with Vm of 48 and 55 mmole acetate produced/min.mg protein, respectively.

Acetyl esterase production by Termitomyces clypeatus

A low molecular weight endo-xylanase (EC 3.2.1.8) was purified from an edible mushroom Termitomyces clypeatus grown in submerged medium with oat spelt xylan. Xylanase was purified to apparent homogeneity by ammonium sulfate fractionation and gel filtration chromatography. Its molecular weight was determined by gel filtration chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be 12 kDa. The enzyme was found to be most active at 50°C and pH 5.0, being most stable at pH 6.5. The Km for oat spelt xylan was determined to be 10.4 mg/ml. The specificities of the enzyme was observed to be highly specific towards oat spelt xylan and was inhibited by mercuric chloride (HgCl2), N-bromosuccinimide, and trans-1,2-diaminocyclohexane-N′,N′,N′,N′-tetraacetic acid strongly. The inhibitory action of N-bromosuccinimide on enzyme confirmed the presence of one tryptophan residue in its substrate-binding site. Amino acid analysis for xylanase showed the presence of high amount of hydrophobic serine, glycine, threonine, and alanine residues. The N-terminal sequencing study for the previously purified and characterized 56 kDa xylanolytic amyloglucosidase reveal the presence of 33.30% identity with glucoamylase chain A from Aspergillus awamori. The N-terminal sequence analysis of the present 12 kDa enzyme showed highest similarity (72.22% identity) towards xylanase from Neurospora crassa.

Subhabrata Sengupta

Papers

Characterization of nimbidiol as a potent intestinal disaccharidase and glucoamylase inhibitor present in Azadirachta indica (neem) useful for the treatment of diabetes

Indian medicinal plants known to contain intestinal glucosidase inhibitors also inhibit pancreatic lipase activity—An ideal situation for obesity control by herbal drugs

Development and Characterization of Carbonic Anhydrase-Based CO 2 Biosensor for Primary Diagnosis of Respiratory Health

Acetyl esterase production by Termitomyces clypeatus

Purification and characterization of a low molecular weight endo-xylanase from mushroom Termitomyces clypeatus.