Metabolism of Free Hydroxyproline in Avena Coleoptiles<sup>*</sup>

Cleland, Robert E.; Olson, Alfred C.

doi:10.1021/bi00853a007

Cited by 23 publications

(24 citation statements)

References 22 publications

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“…Hydroxyproline apparently is a constituent of peroxidase (7,11), but it is not known whether it is necessary for activity of the enzyme. Hydroxyproline is incorporated directly into protein when it is present at growth-inhibiting levels (3,5), and some may be incorporated into peroxidase. It has been suggested that hydroxyproline may render certain cell wall proteins nonfunctional by replacing proline, thereby inhibiting growth (3,6).…”

Section: Resultsmentioning

confidence: 99%

“…Hydroxyproline is incorporated directly into protein when it is present at growth-inhibiting levels (3,5), and some may be incorporated into peroxidase. It has been suggested that hydroxyproline may render certain cell wall proteins nonfunctional by replacing proline, thereby inhibiting growth (3,6). Although this may be the case in structural, hydroxyproline-rich wall proteins, it does not seem to apply to soluble or wall-bound peroxidase.…”

Section: Resultsmentioning

confidence: 99%

“…The tissue was then washed three times with distilled water, which was followed by overnight extraction of I Ohio Agricultural Research and Development Center Journal Paper No. 3 8-70. bound peroxidase with 2 ml of 10 mm Ca(NO. ), solution (9 Wall-bound enzyme was extracted overnight with 3 ml of Ca(NO,)2 solution as described above.…”

Section: Methodsmentioning

confidence: 99%

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Effect of Indoleacetic Acid and Hydroxyproline on Isoenzymes of Peroxidase in Wheat Coleoptiles

Whitmore¹

1971

Plant Physiol.

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Indoleacetic acid at 0.017 millimolar inhibited the formation of three peroxidase isoenzymes in both soluble and wallbound enzyme fractions of wheat coleoptile (Triticum vulgare) tissue. Hydroxyproline at 1 millimolar prevented the indoleacetic acid-induced inhibition. Indoleacetic acid oxidase activity in the soluble fraction was decreased by indoleacetic acid and was restored by hydroxyproline. Most of the indoleacetic acid oxidase activity was located in the electrophoretic zones occupied by two of the peroxidase isoenzymes influenced by indoleacetic acid and hydroxyproline. At least part of the effect of hydroxyproline on auxin-induced elongation of coleoptile tissue may be through control of auxin levels by indoleacetic acid oxidase.Free hydroxyproline inhibits the elongation of excised coleoptiles, especially the elongation induced by IAA (1, 2). Hydroxyproline has been shown recently to occur in peroxidase of some plant tissues (7, 11). Peroxidase may be involved in coleoptile elongation by its action as an IAA oxidase. These observations have prompted an investigation of the effect of IAA and hydroxyproline on peroxidase activity in wheat coleoptiles. MATERIALS AND METHODSAll of the experiments utilized coleoptiles of wheat (Triticum vulgare L. cultivar Redcoat) grown in the dark in vermiculite for 72 hr. Sections, 9 mm long, were cut 3 mm from the tips, and leaves were removed from the coleoptile cylinders.The sections were incubated in groups of 25 for 20 hr on a shaker at 25 C, in darkness. All solutions contained potassium maleate buffer (pH 4.8, 2.5 mm) and sucrose, 50 mm. IAA, when used, was 0.017 mi and hydroxyproline was 1 mM.After incubation, the sections were measured and then ground in a mortar with phosphate buffer, pH 7.0, 67 mm. The tissue was extracted with 10 ml of the phosphate buffer for 1 hr in an ice bath. Solid material was separated by centrifugation at 10OOg for min, and the supernatant was used as the crude, soluble enzyme fraction. This fraction was diluted with 4 volumes of distilled water before peroxidase determinations were made. The tissue was then washed three times with distilled water, which was followed by overnight extraction of bound peroxidase with 2 ml of 10 mm Ca(NO.), solution (9).The calcium treatment released the bound enzyme which was collected in the supernatant by centrifugation and used for peroxidase determinations without dilution. Peroxidase activity was estimated by measuring the increase of absorbance of a mixture containing 2 ml of 120 mi guaiacol and 5 mM H202 in 0.02 M phosphate buffer, pH 5.8, to which was added 0.05 ml of enzyme solution.Peroxidase isoenzymes were separated by starch gel electrophoresis. The procedure given by Ockerse et al. (8) was followed, except that the gel was made with 12 g of starch per 100 ml of buffer. Ten milliliters of soluble enzyme solution, extracted as described above from 60 coleoptile sections per treatment, were dialyzed overnight against distilled water. The dialyzed solutions were freeze-dried and the...

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Effect of Indoleacetic Acid and Hydroxyproline on Isoenzymes of Peroxidase in Wheat Coleoptiles

Whitmore¹

1971

Plant Physiol.

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“…Hydroxyproline of plant tissues has been shown to originate from proline which after incorporation into components of the cell is hydroxylated [ll-131. Free hydroxyproline inhibits both the auxin-induced cell elongation and the formation of protein-bound hydroxyproline [14-171.It will incorporate into plant cells only under special conditions and in small amounts [14,18,19]. I n view of this close association Lamport [3] proposed that hydroxyproline is confined to the cell wall and, consequently, its amount in the plant cell could serve as a measure of the cell wall.…”

mentioning

confidence: 99%

“…It will incorporate into plant cells only under special conditions and in small amounts [14,18,19]. I n view of this close association Lamport [3] proposed that hydroxyproline is confined to the cell wall and, consequently, its amount in the plant cell could serve as a measure of the cell wall.…”

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confidence: 99%

Fractionation and Characterization of Glycoproteins Containing Hydroxyproline from the Leaves of Vicia faba

Pusztai¹,

Watt²

1969

Eur J Biochem

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A survey was conducted of the distribution, solubility, chemical and some physical properties of the constituents of the leaves of Vicia faba containing hydroxyproline. With aqueous trichloroacetic acid about 30OlO of the total leaf hydroxyproline could be brought into solution. The rest remained insoluble in aqueous or non-aqueous solvents tested under non-hydrolytic conditions. The material soluble in trichloroacetic acid was resolved by phenol-aqueous (pH 8) partitioning into (a) predominantly polysaccharide-type materials with small amounts of firmly bound proteins containing hydroxyproline; (b) into some insoluble material and (c) into glycoproteins and glycolipids containing hydroxyproline soluble in the phenol-rich phase, These last were separated into a t least four cationic, one anionic and one stationary components on continuous high voltage electrophoresis in phenol-acetic acid-water. The four cationic glycoprotein fractions were resolved further on the basis of their size on a Bio Gel P 100 column operated in phenol-acetic acid-water. The stationary component was composed of a mixture of glycolipids and contained strongly bound amino acids including hydroxyproline. Analytical results for the major components obtained in this work clearly indicated the presence in the leaves of Vicia faba of a number of glycoproteins, polysaccharide-protein complexes and glycolipids containing hydroxyproline each with characteristic and different composition, molecular size and solubility. Previous work on cell-wall protein (extensin) was discussed in the light of these results.Since the discovery by Steward and Thompson [l] of hydroxyproline in hydrolysates of tissues of plant origin it is now firmly established that this hydroxy imino acid is widely distributed in the plant kingdom. Its occurrence, exact chemical structure and association with other constituents and structural elements of the plant cell have been extensively reviewed [2-41. Hydroxyproline has been reported to be associated with materials in the pericarps and protective seed coats of plants [5-71 and, more specifically, with structural elements of the walls of cultured plant cells [8,9] and of normally grown plant tissues [lo]. Hydroxyproline of plant tissues has been shown to originate from proline which after incorporation into components of the cell is hydroxylated [ll-131. Free hydroxyproline inhibits both the auxin-induced cell elongation and the formation of protein-bound hydroxyproline [14-171.It will incorporate into plant cells only under special conditions and in small amounts [14,18,19]. I n view of this close association Lamport [3] proposed that hydroxyproline is confined to the cell wall and, consequently, its amount in the plant cell could serve as a measure of the cell wall. Recent studies, in addition to some earlier evidence [4], have however cast doubt on the validity of this view. For example, it has since been claimed that collagen is present in plant nuclei [20]. Similarly, in Avena coleoptiles a t least 20°/0 of the total hydro...

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Biochemistry of the Hydroxyprolines

Kuttan¹,

Radhakrishnan²

1973

Advances in Enzymology - And Related Areas of Molecular Biology

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Metabolism of Free Hydroxyproline in Avena Coleoptiles^*

Cited by 23 publications

References 22 publications

Effect of Indoleacetic Acid and Hydroxyproline on Isoenzymes of Peroxidase in Wheat Coleoptiles

Effect of Indoleacetic Acid and Hydroxyproline on Isoenzymes of Peroxidase in Wheat Coleoptiles

Fractionation and Characterization of Glycoproteins Containing Hydroxyproline from the Leaves of Vicia faba

Biochemistry of the Hydroxyprolines

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Metabolism of Free Hydroxyproline in Avena Coleoptiles*

Cited by 23 publications

References 22 publications

Effect of Indoleacetic Acid and Hydroxyproline on Isoenzymes of Peroxidase in Wheat Coleoptiles

Effect of Indoleacetic Acid and Hydroxyproline on Isoenzymes of Peroxidase in Wheat Coleoptiles

Fractionation and Characterization of Glycoproteins Containing Hydroxyproline from the Leaves of Vicia faba

Biochemistry of the Hydroxyprolines

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Metabolism of Free Hydroxyproline in Avena Coleoptiles^*