Determination of radioactive proline and hydroxyproline by a simple paper-chromatographic procedure

Multanen, Veli-Matti; Paunio, Keijo

doi:10.1016/0165-022x(82)90025-2

Cited by 3 publications

(3 citation statements)

References 20 publications

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“…After overnight extraction the bones were washed with 5% TCA, acetone, and ether. The synthesis of collagen and noncoUagen proteins was determined according to Multanen and Paunio (1982).…”

Section: Analysis Of Collagen Synthesismentioning

confidence: 99%

Inhibition of bone collagen synthesis by dental plaque extract

Multanen

Paunio

Larjava

1985

J of Periodontal Research

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Dental plaque extract in low doses inhibited the synthesis of collagen in cultured fetal rat calvaria. Using higher doses of the extract or longer treatment periods the synthesis of noncollagen proteins was also decreased. The denatured extract was as effective as the native one. Although the production of type I collagen in the treated bones was markedly decreased the hydroxylation stage of collagen was not altered. The results suggest that dental plaque extract inhibits the synthesis of collagen by bone cells, which may be one reason for the net loss of collagen of alveolar bone in periodontitis.

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“…After overnight extraction the bones were washed with 5% TCA, acetone, and ether. The synthesis of collagen and noncoUagen proteins was determined according to Multanen and Paunio (1982).…”

Section: Analysis Of Collagen Synthesismentioning

confidence: 99%

Inhibition of bone collagen synthesis by dental plaque extract

Multanen

Paunio

Larjava

1985

J of Periodontal Research

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“…After the reaction, the Hyp appears blackish green and L‐proline turns blue. To discern them, the color reagent II (1.0 g 4‐(dimethylamino)‐benzaldehyde dissolved in 90 mL of acetone and 10 mL of 36% hydrochloric acid) was added in the above reaction liquid, thus making the blackish green into the rosy and washing out the blue . In terms of the principle, the detailed procedure of HTP screening was formulated into two parts, namely, the preparation of a standard colorimetric board and a quantitative assay of Hyp samples.…”

Section: Methodsmentioning

confidence: 99%

Construction and optimization of trans‐4‐hydroxy‐L‐proline production recombinant E. coli strain taking the glycerol as carbon source

Wang

Zhang

Liu

et al. 2016

J of Chemical Tech & Biotech

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BACKGROUND: Trans-4-hydroxy-L-proline (Hyp) is a value-added amino acid that is an applicable chiral building block in some industries, such as the pharmaceutical, cosmetic and healthcare industries. Given that glycerol is a good carbon source for microbial fermentation and a large amount of glycerol is produced by the biodiesel industry, this study investigated a value-added Hyp fermentation from glycerol using an engineered Escherichia coli strain. RESULTS: By optimizing the proline-4-hydroxylase (P4H) gene codons and vectors, a constructed recombinant Escherichia coliBL21 strain successfully converted L-proline to Hyp. With a chemo-physical combination mutagenesis, a high Hyp production strain that can grow with glycerol as a sole carbon source, NA45 was isolated, yielding 1.24 g L −1 from 20 g L −1 glycerol at 12 h in a 30 mL/250 mL conical flask fermentation. With further systemic optimization of nutritional elements, the output was enhanced to 1.62 g L −1 . In a 5 L fermentator, the strain achieved a surprisingly high output of 25.4 g L −1 at 48 h in fed batch mode. CONCLUSION: A high Hyp production strain growing well on glycerol as carbon source was successfully engineered, which is a promising candidate for the industrial Hyp production.

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“…1 bands 1 X 50 em with nbutanoljacetic acid/water (100: 22: 50) solvent. Bands were cut into 0.5 em strips, and counted with ACS [19] in a scintillation counter (Packard). Bands containing standard amino acids were chromatographed in parallel and developed with 0.5% ninhydrin in methanol.…”

Section: Determination Of Specific Activity Of Hydroxyprolinementioning

confidence: 99%

Collagen synthesis in the midgut connective sheath of the mealwormTenebrio molitorL. (Insecta, Coleoptera) during metamorphosis

François

1985

International Journal of Invertebrate Reproduction and Developm

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Internationa/Journal of Invertebrate Reproduction and Development, 8 (1985) 169-174 Elsevier JIR 00270 169 Collagen synthesis in the midgut connective sheath of the meal worm Tenebrio molitor L. (Insecta, Coleoptera) during metamorphosis SummaryThe biosynthesis of the collagen in the mesenteric sheath of the insect mealworm Tenebrio mo/itor L. has been investigated during the last larval, pupal and adult stages. The synthesis of collagenous protein was estimated by the quantitation of proline incorporation into hydroxy[ 3 H]proline in the mesenteron. The maximum conversion of eH]proline into hydroxy[ 3 H]proline occurs in the 5 day old pupa, which appears correlated with the pupal ecdysteroid peak. Relationships between the synthesis of hydroxyproline, histological events and hormonal events are discussed.

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Determination of radioactive proline and hydroxyproline by a simple paper-chromatographic procedure

Cited by 3 publications

References 20 publications

Inhibition of bone collagen synthesis by dental plaque extract

Inhibition of bone collagen synthesis by dental plaque extract

Construction and optimization of trans‐4‐hydroxy‐L‐proline production recombinant E. coli strain taking the glycerol as carbon source

Collagen synthesis in the midgut connective sheath of the mealwormTenebrio molitorL. (Insecta, Coleoptera) during metamorphosis

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