Hydrolysis of L-Ascorbic Acid 2-Sulfate to L-Ascorbic Acid in Freshwater Fishes

Tsujimura, Maki; Fukuda, Tomoko; Kasai, Takeshi; Kitamura, Sasaburo

doi:10.2331/suisan.47.435

Cited by 9 publications

(6 citation statements)

References 4 publications

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“…The experiments indicate antiscorbutic activity of AS in fish, but no authors have reported AS to be equivalent to AA with respect to organ retention of ascorbate (Murai et al 1978;Tsujimura et al 1978;Tsujimura et al 1981;Soliman et al 1986). However, the possible existence of two or more body pools of metabolizeable AA in fish complicates the interpretation of published data due to the methods of analysis applied.…”

Section: Discussionmentioning

confidence: 73%

“…Tucker andHalver (1984, 1986) concluded that AS is stable in feed, readily absorbed and is the major storage form of vitamin C in fish where it is converted to AA as needed to maintain circulating AA levels. However, other studies have indicated that AS may be less efficient than AA as a dietary vitamin C source for rainbow trout (Tsujimura et al 1978), channel catfish (Ictalurus punctatus) (Murai et al 1978), ayu (Plecoglossus altivelis) and tilapia (Oreochromis niloticus) (Tsujimura et al 1981;Soliman et al 1986). In man, guinea pigs and rhesus monkeys AS has been shown to possess little or no vitamin C activity (Kuenzig et al 1974;Machlin et al 1976;Tsujimura et al 1982).…”

Section: Introductionmentioning

confidence: 99%

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Ascorbate-2-sulfate as a dietary vitamin C source for atlantic salmon (Salmo salar): 1. Growth, bioactivity, haematology and humoral immune response

Sandnes

Hansen²,

Killie³

et al. 1990

Fish Physiol Biochem

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The present experiment shows that ascorbate-2-sulfate (AS) is not equivalent to ascorbic acid (AA) as a dietary vitamin C source for Atlantic salmon (Salmo salar). Within reasonable feed supplemental levels AS does not provide the tissues with adequate supplies of vitamin C to secure optimal physiological functions as demonstrated by biochemical and haematological analyses.AS could not be detected in the liver of fish fed either AA or AS, nor in vitamin C - deprived salmon, suggesting that AS is not the natural storage form of vitamin C in this species.There were no significant differences in antibody production against a soluble artificial antigen (NIP11-LPH) in fish fed 500 and 5000 mg AA/Kg dry diet or equivalent amounts of AS during a period of six weeks at a water temperature of 7.2°C.

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Section: Discussionmentioning

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Ascorbate-2-sulfate as a dietary vitamin C source for atlantic salmon (Salmo salar): 1. Growth, bioactivity, haematology and humoral immune response

Sandnes

Hansen²,

Killie³

et al. 1990

Fish Physiol Biochem

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“…The present study suggests that, in rainbow trout, the major physiologic function of C2 sulfatase is to modulate and to maintain adequate cellular levels of C1 consistent with the physiologic requirement of the fish. Rainbow trout and other fishes can survive and grow normally with C2 as the sole dietary source of ascorbate (12,13,29,30). The ubiquitous distribution of C2 in tissues offish (12, t) suggests that this sulfated derivative may be the storage form of C in these animals.…”

Section: Resultsmentioning

confidence: 99%

“…Arylsulfatase activity was first demonstrated in extracts of a marine mollusc (48) and later in other aquatic organisms (13,38,41,49). Widespread distribution of arylsulfatases was established as the enzyme was detected and purified from a num-ber of organisms living in different environments varying in physiologic complexity from microorganisms to man.…”

Section: Resultsmentioning

confidence: 99%

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Ascorbic acid sulfate sulfohydrolase (C2 sulfatase): the modulator of cellular levels of L-ascorbic acid in rainbow trout.

Benitez¹,

Halver²

1982

Proc. Natl. Acad. Sci. U.S.A.

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The enzyme L-ascorbic acid 2-sulfate sulfohydrolase (C2 sulfatase) was purified from rainbow trout liver. The enzyme catalyzes the hydrolysis of L-ascorbic acid 2-sulfate and has a pH optimum at 6.0. It has a molecular weight of about 117,500 at pH 5.0 and is inhibited by a number of sulfhydryl blocking agents including L-ascorbic acid. C2 sulfatase activity was observed in most metabolic organs of rainbow trout. These findings suggest that the physiologic role of the enzyme is to maintain adequate cellular concentrations of L-ascorbic acid in the fish. The activity of the enzyme is controlled by L-ascorbic acid through feedback inhibition. Comparison of kinetic constants and inhibition patterns suggests that C2 sulfatase is structurally identical to human arylsulfatase A. However, unlike C2 sulfatase, human arylsulfatase A may not be involved in ascorbate metabolism. Its physiologic substrate is reported to be cerebroside-3-sulfate, not L-ascorbic acid 2-sulfate. A scheme is proposed to account for the functional divergence of these two structurally identical enzymes.L-Ascorbic acid (C1) plays a critical role in all living organisms. Trout, salmon, and a number of other fish species (1-6) have a dietary requirement for C1. As in mammalian systems, C1 appears to be involved in collagen synthesis. Fish reared on C1-deficient diets develop signs traceable to impaired collagen biosynthesis; i.e., lordosis, scoliosis, vertebral dislocation, deformation of support cartilage, and delayed wound repair (4-6).C1 is the most chemically unstable component of fish feeds. L-Ascorbic acid 2-sulfate (C2), a more stable derivative of C1 was discovered in brine shrimp cyst (Artemia salina) (7,8). It was also detected as a metabolite in human urine (9) and in the liver, spleen, adrenal glands, and bile of rats (10, 11). C2 promptly arrested signs of fish scurvy in rainbow trout reared on a scorbutic diet (12). In a group ofrainbow trout fed for 1 yr an artificial diet containing C2 as sole source of ascorbate, normal growth, diet efficiency, and absence of scurvy indicated that C2 sulfate was an adequate source of C1.Enzymatic hydrolysis of C2 to C1 by a sulfohydrolase would be a critical step in the utilization ofC2 as a vitamin source. This activity has been detected in fish tissues (12, 13), in the liver of the gastropod Charonia lampas (14), and in extracts of mammalian tissues (15,16). The ability ofrainbow trout to utilize C2 as sole dietary source ofC makes this fish a model test organism for the study of the sulfatase. This paper deals with the purification and properties of C2 sulfohydrolase (C2 sulfatase) from rainbow trout liver. Experimental evidence suggests that the enzyme modulates cellular levels of C1 in the fish.MATERIALS AND METHODS Materials. Ultrapure grade C1 was from Hoffmann-La Roche. The dipotassium salt of C2 was generously donated by Paul A. Seib (Kansas State University). Dipotassium 4-nitrocatechol sulfate, crystalline 4-nitrocatechol, crystallized and lyophilized bovine serum albumin, apofer...

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The effect of varying forms of dietary ascorbic acid on the nutrition of juvenile tilapias (Oreochromis niloticus)

1986

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Hydrolysis of L-Ascorbic Acid 2-Sulfate to L-Ascorbic Acid in Freshwater Fishes

Cited by 9 publications

References 4 publications

Ascorbate-2-sulfate as a dietary vitamin C source for atlantic salmon (Salmo salar): 1. Growth, bioactivity, haematology and humoral immune response

Ascorbate-2-sulfate as a dietary vitamin C source for atlantic salmon (Salmo salar): 1. Growth, bioactivity, haematology and humoral immune response

Ascorbic acid sulfate sulfohydrolase (C2 sulfatase): the modulator of cellular levels of L-ascorbic acid in rainbow trout.

The effect of varying forms of dietary ascorbic acid on the nutrition of juvenile tilapias (Oreochromis niloticus)

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