Reexamination of the amino acid compositions of proteins from penaeid shrimp: failure to find uncommonly-high tryptophan levels

Raymond C. Duhamel, Michael Finerty, Donald V Lightner, Klaus Brendel

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Abstract

1. 1. A soluble fraction and an insoluble fraction were isolated from cuticle-free tail tissue of Penaeus vannamei and their amino acid compositions compared to analogous fractions previously isolated from Penaeus setiferus by Thompson & Thompson (Comp. Biochem. Physiol. 27, 127-132 (1968); 35, 471-477 (1970)) in which tryptophan contents of 119.3 and 190.4 residues/1000 were reported. 2. 2. The previously-reported tryptophan values are surprisingly high, because tryptophan is generally the least abundant amino acid in proteins. In this study, a maximum of 9.7 tryptophan residues/1000 were found. 3. 3. Extraction with 1 M NaCl followed by 0.5 M acetic acid solubilized 94% of the total protein but no hydroxyproline, indicating that shrimp collagen is uniformly insoluble, perhaps because of extensive cross-linking.

Original languageEnglish (US)
Pages (from-to)301-304
Number of pages4
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume73
Issue number2
DOIs
StatePublished - 1982

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Penaeidae
Tryptophan
Amino Acids
Chemical analysis
Proteins
Hydroxyproline
Acetic Acid
Tail
Collagen
Tissue

Cite this

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title = "Reexamination of the amino acid compositions of proteins from penaeid shrimp: failure to find uncommonly-high tryptophan levels",
abstract = "1. 1. A soluble fraction and an insoluble fraction were isolated from cuticle-free tail tissue of Penaeus vannamei and their amino acid compositions compared to analogous fractions previously isolated from Penaeus setiferus by Thompson & Thompson (Comp. Biochem. Physiol. 27, 127-132 (1968); 35, 471-477 (1970)) in which tryptophan contents of 119.3 and 190.4 residues/1000 were reported. 2. 2. The previously-reported tryptophan values are surprisingly high, because tryptophan is generally the least abundant amino acid in proteins. In this study, a maximum of 9.7 tryptophan residues/1000 were found. 3. 3. Extraction with 1 M NaCl followed by 0.5 M acetic acid solubilized 94{\%} of the total protein but no hydroxyproline, indicating that shrimp collagen is uniformly insoluble, perhaps because of extensive cross-linking.",
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T1 - Reexamination of the amino acid compositions of proteins from penaeid shrimp

T2 - failure to find uncommonly-high tryptophan levels

AU - Duhamel, Raymond C.

AU - Finerty, Michael

AU - Lightner, Donald V

AU - Brendel, Klaus

PY - 1982

Y1 - 1982

N2 - 1. 1. A soluble fraction and an insoluble fraction were isolated from cuticle-free tail tissue of Penaeus vannamei and their amino acid compositions compared to analogous fractions previously isolated from Penaeus setiferus by Thompson & Thompson (Comp. Biochem. Physiol. 27, 127-132 (1968); 35, 471-477 (1970)) in which tryptophan contents of 119.3 and 190.4 residues/1000 were reported. 2. 2. The previously-reported tryptophan values are surprisingly high, because tryptophan is generally the least abundant amino acid in proteins. In this study, a maximum of 9.7 tryptophan residues/1000 were found. 3. 3. Extraction with 1 M NaCl followed by 0.5 M acetic acid solubilized 94% of the total protein but no hydroxyproline, indicating that shrimp collagen is uniformly insoluble, perhaps because of extensive cross-linking.

AB - 1. 1. A soluble fraction and an insoluble fraction were isolated from cuticle-free tail tissue of Penaeus vannamei and their amino acid compositions compared to analogous fractions previously isolated from Penaeus setiferus by Thompson & Thompson (Comp. Biochem. Physiol. 27, 127-132 (1968); 35, 471-477 (1970)) in which tryptophan contents of 119.3 and 190.4 residues/1000 were reported. 2. 2. The previously-reported tryptophan values are surprisingly high, because tryptophan is generally the least abundant amino acid in proteins. In this study, a maximum of 9.7 tryptophan residues/1000 were found. 3. 3. Extraction with 1 M NaCl followed by 0.5 M acetic acid solubilized 94% of the total protein but no hydroxyproline, indicating that shrimp collagen is uniformly insoluble, perhaps because of extensive cross-linking.

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