Primary Structure

Piez, Karl A.

doi:10.1007/978-1-4757-4602-0_1

Cited by 68 publications

(26 citation statements)

References 77 publications

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“…In bone, collagen type I is the most abundant protein and commonly used for reconstructing palaeodiet (Ambrose 1990). Collagen type I is a triple helix (Ramachandran et al 1968;Bornstein and Traub 1979;Piez 1976) and contains two alpha 1 and one alpha 2 helices (Piez 1984). The alpha 1 and alpha 2 chains differ only slightly and consist mainly of triplets with the order Gly-X-Y (where X stands for proline and Y for hydroxyproline); all other amino acids are less well represented (Piez 1976).…”

Section: Introductionmentioning

confidence: 99%

“…Collagen type I is a triple helix (Ramachandran et al 1968;Bornstein and Traub 1979;Piez 1976) and contains two alpha 1 and one alpha 2 helices (Piez 1984). The alpha 1 and alpha 2 chains differ only slightly and consist mainly of triplets with the order Gly-X-Y (where X stands for proline and Y for hydroxyproline); all other amino acids are less well represented (Piez 1976). The intracellular translated and post-translationally modified collagen fibres are transported into the intercellular space and are then organised into fibrils (Reddi 1984).…”

Section: Introductionmentioning

confidence: 99%

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Establishing collagen quality criteria for sulphur isotope analysis of archaeological bone collagen

Nehlich

Richards

2009

Archaeol Anthropol Sci

237

192

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Sulphur isotope measurements of bone collagen from archaeological sites are beginning to be applied more often, yet there are no clear criteria to assess the quality of the collagen and therefore the validity of the sulphur isotope values. We provide elemental data from different methods (DNA sequences, amino acid sequences and mass spectrometric measurements) which are used to establish a reliable system of quality criteria for sulphur isotope analyses of bone collagen. The difference in the amount of sulphur from fish and mammalian collagen type I led to the suggestion to use different criteria to assess the in vivo character of the collagen between these two categories. For establishing quality ranges, the bone collagen of 140 modern animals were analysed. The amount of sulphur in fish and mammalian bone collagen is 0.63±0.08% and 0.28 ±0.07%, respectively. Based on these results we define for mammalian bone collagen an atomic C:S ratio of 600±300 and an atomic N:S ratio of 200±100, and for fish bone an atomic C:S ratio of 175±50 and an atomic N:S ratio of 60± 20. These quality criteria were then applied to 305 specimens from different archaeological contexts.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Establishing collagen quality criteria for sulphur isotope analysis of archaeological bone collagen

Nehlich

Richards

2009

Archaeol Anthropol Sci

237

192

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“…Interstitial collagens (types I-III [7]), in contrast, contain no more than 1-2 residues of 3-hydroxyproline/1,000. In the completely sequenced a-I chain of type I collagen (8), the single residue of 3-hydroxyproline is present in the sequence Gly-3-Hyp-4-Hyp; the same tripeptide Received for publication 27 December 1977. sequence appears also to account for all or most of the 3-hydroxyproline in basement membrane collagen of kidney cortex (9).…”

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confidence: 99%

3-Hydroxyproline content of normal urine.

Adams¹,

Ramaswamy²,

Lamon³

1978

J. Clin. Invest.

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A B S T R A C T Values for total 3-hydroxyproline and 4-hydroxyproline were obtained from 24-h urine specimens of 18 healthy human subjects ofboth sexes, whose ages ranged from the first to the sixth decade in age. Urinary 3-hydroxyproline levels, not earlier described to our knowledge, were determined by an isotope-dilution method requiring considerable purification and utilizing the amino acid analyzer for final measurement. 3-Hydroxyproline averaged 3% of the corresponding 4-hydroxyproline in individual urine samples. Like 4-hydroxyproline, 3-hydroxyproline excretion is increased in the second decade, and there is generally good correlation between the two values in individual urines. A hydroxyprolinemic subject excreting greatly elevated 4-hydroxyproline levels did not excrete excessive 3-hydroxyproline, consistent with independent catabolic pathways for the two compounds.3-Hydroxyproline appears to be selectively excreted relative to 4-hydroxyproline when compared with the probable total body content of each amino acid. Possible explanations are: a more rapid turnover of basement membrane collagen than interstitial collagen or, alternatively, relatively greater resistance to the proteolytic cleavage of peptides containing 3-hydroxyproline.

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“…These results are not surprising if it is recalled that: (i) the 3-D assembly of proteins depends primarily on their amino acid sequence; (ii) the sequence of a given type of collagen (Type I, II, III or IV) varies little from one species to another [13,14]. Hence we may expect that, unless influenced by other molecules, collagen will assemble in the same way in different tissues.…”

Section: Discussionmentioning

confidence: 99%