TY - JOUR
T1 - Ascorbic acid-dependent collagen formation in penaeid shrimp
AU - Hunter, B.
AU - Magarelli, P. C.
AU - Lightner, D. V.
AU - Colvin, L. B.
PY - 1979
Y1 - 1979
N2 - 1. 1. This study tested the hypothesis that black death, the ascorbic acid (AsA) related disease of penaeid shrimp, is related to collagen underhydroxylation. 2. 2. Collagen measured as hydroxyproline (HYP) in healthy Penaeus californiensis (Holmes) and P. stylirostris (Stimpson) of a wide range of masses was determined. The results revealed a logarithmic relationship between total body collagen HYP and body weight fitting the equation y = 90×1.18 where y = total collagenous HYP (μg) and x = body weight (g). 3. 3. Shrimp tissues most subject to mechanical trauma (subcutis, hindgut and gills) had the highest collagenous HYP levels and were most consistently and severely affected by an ascorbic acid (AsA) deficiency disease. 4. 4. Prolyl hydroxylase (PH) activity was demonstrated in tissues of P. californiensis and P. stylirostris by hydroxylation of [3,4-3H]proline. 5. 5. AsA was required for shrimp PH activity using a chicken embryo substrate. 6. 6. Nutritional trials revealed that dietary AsA was required for proline hydroxylation in collagen formation in P. californiensis.
AB - 1. 1. This study tested the hypothesis that black death, the ascorbic acid (AsA) related disease of penaeid shrimp, is related to collagen underhydroxylation. 2. 2. Collagen measured as hydroxyproline (HYP) in healthy Penaeus californiensis (Holmes) and P. stylirostris (Stimpson) of a wide range of masses was determined. The results revealed a logarithmic relationship between total body collagen HYP and body weight fitting the equation y = 90×1.18 where y = total collagenous HYP (μg) and x = body weight (g). 3. 3. Shrimp tissues most subject to mechanical trauma (subcutis, hindgut and gills) had the highest collagenous HYP levels and were most consistently and severely affected by an ascorbic acid (AsA) deficiency disease. 4. 4. Prolyl hydroxylase (PH) activity was demonstrated in tissues of P. californiensis and P. stylirostris by hydroxylation of [3,4-3H]proline. 5. 5. AsA was required for shrimp PH activity using a chicken embryo substrate. 6. 6. Nutritional trials revealed that dietary AsA was required for proline hydroxylation in collagen formation in P. californiensis.
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U2 - 10.1016/0305-0491(79)90286-4
DO - 10.1016/0305-0491(79)90286-4
M3 - Article
C2 - 233793
AN - SCOPUS:0018635048
VL - 64
SP - 381
EP - 385
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
SN - 1096-4959
IS - 4
ER -