Anti-tyrosinase, anti-elastase, and antioxidant activities of some symmetric bisthiocarbohydrazone compounds

Symmetric bisthiocarbohydrazone compounds (1, 2, 3) were obtained by the condensation of thiocarbohydrazide with carbonyl compounds such as isatin (a heterocyclic ketone) and two hydroxyl aldehydes (2-hydroxybenzaldehyde, 2-hydroxy-1-naphthaldehyde) respectively, according to the previously reported methods. These synthesized compounds were evaluated in terms of their anti-tyrosinase, anti-elastase and antioxidant potentials in vitro. All of the tested compounds exhibited anti-tyrosinase and anti-elastase activities. It was observed that the inhibition increased with the increase of bisthiocarbohydrazone concentrations. Compound 1 showed the highest anti-tyrosinase activity. The anti-tyrosinase activity is decreasing in the following order; 2<3<1. Compound 1 showed also the highest anti-elastase activity. The anti-elastase activity is decreasing as 3<2<1. As a result, the most effective compound in terms of anti-tyrosinase and anti-elastase activities is bisthiocarbohydrazone derived from isatin. Compounds 2 and 3 with the hydroxyl substitution showed antioxidant activity close to Trolox. These compounds were found to have significant reducing effects and to be effective scavengers of DPPH

Antioxidant and antiacetylcholinesterase activities of chard (Beta vulgaris L. var. cicla)

Plants have been used for many years as a source of traditional medicine to treat various diseases and conditions. Many of these medicinal plants are also excellent sources for phytochemicals, many of which contain potent antioxidant and antiacetylcholinesterase activities. Chard (Beta vulgaris L var. cicla) is widely spread in Turkey and used as an antidiabetic in traditional medicine. In the present study, the antioxidant activity and acetylcholinesterase inhibitor capacity of chard were examined. In addition, proline level of chard was determined. The antioxidant activity of water extract of chard was evaluated using different antioxidant tests. The results were compared with natural and synthetic antioxidants. The results suggest that chard may provide a natural source of antioxidant and antiacetylcholinesterase activities and proline content. (C) 2010 Elsevier Ltd. All rights reserved

Purification and some properties of rose (Fructus cynosbati) hips invertase

lnvertase was purified from rose (Fructus cynosbati) hips by ammonium sulfate fractionation and hydroxyapatite column chromatography. The enzyme was obtained with a yield of 4.25% and about 10.48-fold purification and had a specific activity of 8.59 U/mg protein. The molecular mass of invertase was estimated to be 66.51 kDa by PAGE and 34 kDa by SDS-PAGE, indicating that the native enzyme was a homodimer. The enzyme was a glycoprotein and contained 5.86% carbohydrate. The K-m for sucrose was 14.55 mM and the optimum pH and temperature of the enzyme were 4.5 and 40 degrees C, respectively. Sucrose was the most preferred substrate of the enzyme. The enzyme also hydrolyzed D(+) raffinose, D(+) trehalose and inulin (activity 39.88, 8.12 and 4.94%, respectively of that of sucrose), while D(+) lactose, cellobiose and D(+) maltose showed no effect on the enzyme. The substrate specificity was consistent with that for a beta-fructofuranoside, which is the most popular type in the higher plants. The enzyme was completely inhibited by HgCl2, MnCl2, MnSO4, FeCl3, Pb(NO3)(2), ammonium heptamolybdate, iodoacetamide and pyridoxine hydrochloride. It was also inhibited by Ba(NO3)(2) (86.32%), NH4Cl (84.91%), MgCl2 (74.45%), urea (71.63%), l(2) (69.64%), LiCl (64.99%), BaCl2 (50.30%), Mg(NO3)(2) (49.90%), CrCl3 (31.90%) and CuSO4 (21.45%) and but was activated by Tris (73.99%) and methionine (12.47%)

Purification and some properties of rose (<i style="">Fructus cynosbati)</i> hips invertase

109-114Invertase was purified from rose (Fructus cynosbati) hips by ammonium sulfate fractionation and hydroxyapatite column chromatography. The enzyme was obtained with a yield of 4.25% and about 10.48-fold purification and had a specific activity of 8.59 U/mg protein. The molecular mass of invertase was estimated to be 66.51 kDa by PAGE and 34 kDa by SDS-PAGE, indicating that the native enzyme was a homodimer. The enzyme was a glycoprotein and contained 5.86% carbohydrate. The Km for sucrose was 14.55 mM and the optimum pH and temperature of the enzyme were 4.5 and 40°C, respectively. Sucrose was the most preferred substrate of the enzyme. The enzyme also hydrolyzed D(+) raffinose, D(+) trehalose and inulin (activity 39.88, 8.12 and 4.94%, respectively of that of sucrose), while D(+) lactose, cellobiose and D(+) maltose showed no effect on the enzyme. The substrate specificity was consistent with that for a β-fructofuranoside, which is the most popular type in the higher plants. The enzyme was completely inhibited by HgCl2, MnCl2, MnSO4, FeCl3, Pb(NO3)2, ammonium heptamolybdate, iodoacetamide and pyridoxine hydrochloride. It was also inhibited by Ba(NO3)2 (86.32%), NH4Cl (84.91%), MgCl2 (74.45%), urea (71.63%), I2 (69.64%), LiCl (64.99%), BaCl2 (50.30%), Mg(NO3)2 (49.90%), CrCl3 (31.90%) and CuSO4 (21.45%) and but was activated by Tris (73.99%) and methionine (12.47%)

Effects of Melissa officinalis L. extract on the skin tissues of hyperlipidemic rats

In this study, the effects of Melissa officinalis L. on hyperlipidemic rats were investigated biochemically. The animals were fed a lipogenic diet consisting of 2 % cholesterol, 20 % sunflower oil and 0.5 % cholic acid added to normal chow and were given 3 % ethanol for 42 d. The extract was given gavage technique to rats a dose of 2 g/kg everyday for 28 d, after 14 d, experimental animals done hyperlipidemia. In hyperlipidemic groups, a reduction of the skin glutathione level (GSH), skin superoxide dismutase (SOD) activity and serum catalase (CAT), paraoxonase (PON) activity and an increase in serum cholesterol, total lipid, triglycerides and uric acid, gamma-glutamyl transferase activity (GGT) and skin cholesterol, total lipid, lipid peroxidation (LPO), nonenzymatic glycosylation (NEG) and skin CAT, lactate dehydrogenase (LDH), glutathione peroxidase (GP,) and myeloperoxidase (MPO) activity were observed. Treatment with Melissa officinalis L. extract reversed these effects. Present results show that Melissa officinalis L. extract has a protective effect against skin tissue damage as result of hyperlipidemia, in addition to hypolipidemic effect

<em>In vitro</em> inhibitory effect of <em>Aloe vera</em> (L.) Burm. f. leaf extracts on the activity of some enzymes and antioxidant activity

82-89Aloe vera (L.) Burm. f. possess succulent leaves which gel or whole extracts are commercially used in cosmetic industry as well as a food supplement for its multiple health benefits. Research for medicines based on the inhibition mechanism of enzymes is a promising topic. In this study, four different enzymes were chosen: Elastase, neuraminidase, ɑ-amylase, and lipase. In addition, the antioxidant activities of leaf skin and gel extracts of A. vera were evaluated using reducing power, DMPD, and NO radical scavenging activities. A. vera leaves were collected from the plant which is cultivated in the greenhouse of Istanbul University, Alfred Heilbronn Botanical Garden. The leaf gel and skin were homogenized in phosphate buffered saline.Among the four enzymes, A. vera leaf gel and skin extracts showed the best inhibition of elastase and ɑ-amylase and moderated inhibitory activity for neuraminidase and lipase. A. vera leaf gel and skin extracts showed the best activity of DMPD radical scavenger and moderate NO scavenging activity and reducing power.The results suggested that A. vera extracts may provide a natural source of anti-elastase, antilipase and ɑ-amylase and neuraminidase inhibitory activities and that they are a natural source of antioxidant

In vitro inhibitory effect of Aloe vera (L.) Burm. f. leaf extracts on the activity of some enzymes and antioxidant activity

Aloe vera (L.) Burm. f. possess succulent leaves which gel or whole extracts are commercially used in cosmetic industry as well as a food supplement for its multiple health benefits. Research for medicines based on the inhibition mechanism of enzymes is a promising topic. In this study, four different enzymes were chosen: Elastase, neuraminidase, alpha-amylase, and lipase. In addition, the antioxidant activities of leaf skin and gel extracts of A. vera were evaluated using reducing power, DMPD, and NO radical scavenging activities. A. veraleaves were collected from the plant which is cultivated in the greenhouse of Istanbul University, Alfred Heilbronn Botanical Garden. The leaf gel and skin were homogenized in phosphate buffered saline. Among the four enzymes, A. vera leaf gel and skin extracts showed the best inhibition of elastase and alpha-amylase and moderated inhibitory activity for neuraminidase and lipase. A. vera leaf gel and skin extracts showed the best activity of DMPD radical scavenger and moderate NO scavenging activity and reducing power. The results suggested that A. vera extracts may provide a natural source of anti-elastase, antilipase and alpha-amylase and neuraminidase inhibitory activities and that they are a natural source of antioxidant