PARTIAL PURIFICATION AND EFFECT OF TEMPERATURE AND HEAT STABILITY STUDIES ON RHODANESE FROM THE LIVER OF A LOCAL GOAT

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✎: PARTIAL PURIFICATION AND EFFECT OF TEMPERATURE AND HEAT STABILITY STUDIES ON RHODANESE FROM THE LIVER OF A LOCAL GOAT

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Keywords: PARTIAL PURIFICATION AND EFFECT OF TEMPERATURE AND HEAT STABILITY STUDIES ON RHODANESE FROM THE LIVER OF A LOCAL GOAT

 

RESEARCH BODY

ABSTRACT

The research is aimed at investigating the effect of temperature and heat stability of Rhodanese from the Liver of a local goat.                                   This research shows the existence of rhodanese from a local goat liver homogenate. It was observed that the enzyme was partially purified by ammonium sulphate precipitation and dialysis. The specific activity of enzyme after partial purification using ammonium sulphate precipitation and dialysis was 4.39 U/mg.  The effect of temperatures between 30 and 80C on the rhodanese activity showed that optimum temperature for the enzyme was at 60C. It was found that the enzyme (rhodanese) from a local goat liver was stable at 60C, but was unstable at temperatures 70C.

CHAPTER ONE

1.0                                                                                            INTRODUCTION

The role of rhodanese in different parts of the animal and perhaps in plants is controversial; particularly its function in the detoxification of acute cyanide exposure (Delvin et al., 1989; Sylvester and Sander, 1990). Rhodanese is a sulphur transferase that catalyses, in vitro, the formation of thiocyanate from cyanide and thiosulphate or other suitable sulphur donors. In vivo the enzyme is, however multifunctional (Smith and Urbanska, 1986).

It is generally believed that the major function of rhodanese is cyanide detoxification (Smith and Urbanska, 1986; Buzaleh et al., 1990). This function is more prominent in mammals where highly cytotoxic cyanide is converted to a less toxic thiosulphate and excreted through the kidney (Cagianut et al., 1984; Keith et al., 1989; Bourdoux et al., 1980). In plants, a

close relationship exists between rhodanese activity and cyanogenesis, which suggest that the enzyme provides a mechanism for cyanide detoxification in cyanogenic plants (Smith and Urbanska, 1986).

The capacity of Bacillus stearothermophilus to detoxify cyanide could be greatly increased when mutants containing 5 to 6 times rhodanese activity of

normal cells were used (Atkinson, 1971).

The distribution of rhodanese in both adult and larvae insects is not restricted to those species that encounter exogenous cyanide through feeding on cyanogenic plants (Beesley et al., 1985). This is an indication that cyanide detoxification may not be the primary role of this enzyme in insects. In insects, it was proposed that the enzyme might be involved in a more important role of sulphur transfer for protein synthesis. In squid (Loligo

peali), it is more likely to be involved in the formation of C-S bond of isethionate, which is present to the concentration o f 150 mM in its giant axon (Hoskin and Kordik, 1977). In Rhodopseudomonas spheroids rhodanese catalyse the formation of cysteine from cysteine trisulphide (Dexifra et al., 1975). Rhodanese in its phosphorylated and dephosphorylated forms has been reported to function as a converter enzyme that interact with mitochondrial membrane bound iron–sulphur centers of the

mitochondrial electron transport chain where it modulate the rate of respiration (Ogata and Volina, 1990). There is an indication of a possible role of rhodanese in providing labile sulphide necessary for the synthesis of ferredoxin in the chloroplast of spinach, parsley, cabbage, and red turnips (Tomati, 1972). It also catalyses the formation of iron-sulphur centers in

Escherichia coli, and a physiological role of the enzyme in aerobic metabolism in this organism was suggested (Keith and Volina, 1987).

Rhodanese was also reported to reconstitute spinach ferredoxin (Pagani et al., 1984); restore durum wheat leaves cyanide inactivated NADH: nitrate reductase activity and if added before cyanide treatment, it protects the enzyme (Tomati et al., 1976). It also restore, partially, the activity of NADH dehydogenase (Pagani and Galante, 1983). It was also fund to increase the activity of malate dehydrogenase (Agro et al., 1976). Restoration of MgATP and chelator inactivated nitrogenase of Klebsiella pneumoniae has been reported (Pagani et al., 1987). A possible role of the enzyme in modulating S-amino levulinate synthetase activity has also been reported (Vazquez et

al., 1987). In Thiobacillus intermedius, the mechanism of oxidation of thiosulphate to sulphate seems to involve the action of rhodanese (Charles, 1969). At pH 8.8 beef liver rhodanese however catalyses the reduction of thiosulphate to sulphite (Koj, 1968). Its activity was also related to the oxidation of thiosulphate and elemental sulphur to sulphate by the fungus, Rhizopus oryzae (Ray et al., 1990). The presence of rhodanese has been detected in many tissues of animals (Dudeck et al., 1980; Westley 1981; Drawbaugh and Marrs, 1987), but there is no information about the activity of rhodanese in Japanese quail and partridge tissues and little information about tissue distribution of this enzyme in pigeon.

Its occurrence in the roots of plants has been reported (Castella, 1954). In bacteria, rhodanese has been shown to be present in Escherichia coli (Stearns, 1953), Thiobacillus thiocyanoxidars (Mc- Chesney, 1957) and T. denitriftcan (Woolley, 1961). The formation of CNS- from colloidal sulphur and CN- is catalysed by a different enzyme, rhodanese S, present in blood serum (Sorbo, 1955). The biological role of rhodanese is not clear, although its possible function in cyanide detoxification has been repeatedly stressed. Rhodanese and thiosulphate added to cyanide-inhibited cytochrome c oxidase give a rapid reactivation of the latter enzyme (Sorbo, 1957). The inhibition of cytochrome oxidase is the chief reason for the high toxicity of cyanide, since the cyanide complex can no longer act as an electron acceptor in the chain (West & Todd, 1961). No differences were observed in a comparison of rhodanese from liver and kidney (Westley, 1959).

Rhodanese is widely distributed in both plants and animal species. Two forms of rhodanese, have been demonstrated. These forms are dephospho– and phospho– rhodanese. They were identical with respect to kinetic parameters, amino acid composition amino terminal amino acid, sulphahydryl content, tryptic maps and molecular weights (Aminlari and Gilanpour, 1991; Aminlari and Shahbazi, 1994).                                               Goat is a member of the family Bovidae and is closely related to the sheep as both are in the goat-antelope subfamily Caprinae. There are over 300 distinct breeds of goat (Taylor and Field, 1999). Goat is one of the oldest domesticated species, and has been used for their milk, meat, hair and skins over much of the world.        The goat comprises of different organs, one of which is liver.                                                                                                  The liver is a vital organ of the digestive system present in vertebrates and some other animals. It has a wide range of functions, including detoxification, protein synthesis, and production of biochemicals necessary for digestion (Maton et al., 1993). The liver is necessary for survival; there is currently no way to compensate for the absence of liver function in the long term, although new liver dialysis techniques can be used in the short term. This gland plays a major role in metabolism and has a number of functions in the body, including glycogen storage, decomposition of red blood cells, plasma protein synthesis, hormone production, and detoxification (Kmieć, 2001).

1.1     AIM OF RESEARCH

The aim of this research is to investigate the effect of temperature and heat stability of Rhodanese from the Liver of a local goat.

 

Keywords: PARTIAL PURIFICATION AND EFFECT OF TEMPERATURE AND HEAT STABILITY STUDIES ON RHODANESE FROM THE LIVER OF A LOCAL GOAT

 


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Keywords: PARTIAL PURIFICATION AND EFFECT OF TEMPERATURE AND HEAT STABILITY STUDIES ON RHODANESE FROM THE LIVER OF A LOCAL GOAT

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