An arabinogalacto(4-O-methylglucurono)xylan from the leaves of Hordeum vulgare

An arabinogalacto(4-O-methylglucurono)xylan with a $\text{DP}$_n of ca. 96 has been isolated from the leaves of barley. Based on structural studies it is proposed that the hemicellulose consists of a main chain of β (1→4)-linked d-xylopyranosyl residues to which are attached an average of 8·1 l-arabinofuranosyl residues, 3·8 galactopyranosyl-(1→4)-d-xylopyranosyl-(1→2)-l-arabinofuranosyl residues and 4·4 4-O-methyl-d-glucopyranuronosyl residues.     

Barley proteinase inhibitors: A possible role in grasshopper control?

Young growing barley seedlings contain trypsin and chymotrypsin proteinase inhibitors in their leaf juices. The amount of chymotrypsin inhibitor varies greatly while trypsin inhibitor content is nearly the same in all varieties tested. Compana (CI5438) barley has much more total inhibitor than does Trebi (CI 936), Titan (CI 7055), Horn (CI 926), Hiproly (CI 3947) and Hiproly Normal (CI 4362). The distribution of inhibitors in different barley varieties correlates with the severity of grasshopper damage observed by other workers. Barley leaves could not be induced to accumulate proteinase inhibitors after excision and incubation, wounding, or absorption of crude “proteinase inhibitor inducing factor” preparations. Grasshopper damage experiments as related to proteinase inhibitor should be done in the field using yield as the correlative factor.     

Degradation of [α-14C]hordenine in Hordeum vulgare plants

Evidence is presented indicating that intact plants of Hordeum vulgare degrade [α- ¹⁴C]hordenine to ¹⁴CO ₂.     

Carnitine content of greening Barley leaves

The carnitine content of etiolated barley leaves doubled on exposure to light. After 24 hr exposure the carnitine content was the same as that of barle     

Conversion of saccharopine to lysine in barley

Labelled saccharopine was synthesized and showed a low conversion to lysine in barley seedlings. The results indicate a role of saccharopine in either lysine biosynthesis or catabolism.     

Metabolism of gramine in Hordeum vulgare plants: A time course study

Intact Hordeum vulgare plants quantitatively degrade [α-¹⁴C] gramine to ¹⁴CO₂.     

Serological characterization of a ribonuclease from Hordeum vulgare

Specific rabbit antisera against purified Hordeum vulgare seedling RNase I from two winter barley cultivars each formed a single precipitin band when reacted with the homologous crude tissue extract. RNase antigen from either cultivar was equally reactive with both antisera when evaluated by immunodiffusion and immunoelectrophoresis. A small but consistent difference in anti-RNase specificity between cultivars was shown by passive hemagglutination inhibition, suggesting that molecular differences may exist between the two RNase antigens. Immunodiffusion and rocket immunoelectrophoresis were used to qualitatively test the cross-reactivity of protein preparations from various members of the genus Hordeum and species from other related grass genera. Neither antiserum showed cross-reactivity with soluble protein preparation from species outside the genus Hordeum. A few species within the genus Hordeum were cross-reactive. A modification of rocket immunoelectrophoresis was developed to determine the amount of RNase in unpurified tissue extracts. The technique involved a template-reservoir which allowed detection of 250 ng RNase in tissue extract volumes of 50 μl. The amount of RNase in unpurified protein extracts from the two cultivars of barley was similar.     

Characterisation of the endospermal trypsin inhibitor of barley

A trypsin inhibitor was isolated from grains of two row barley (cv. Proctor). The purified protein was identical with the corresponding inhibitor of a six row barley (cv. Pirkka); both proteins showed, a Pi of 7.4. The N-terminal amino acid was phenylalanine and an arginine residue was involved in the active site. Effects of substrate concentration showed that the inhibition was noncompetitive with a K_i of about 0.9 × 10^?7M. An enzyme-inhibitor complex was demonstrated by disc electrophoresis.     

Purification and properties of a β-N-acetylaminoglucohydrolase from malted barley

β-N-Acetylaminoglucohydrolase (β-2-acetylamino-2-deoxy-D-glucoside acetylaminodeoxyglucohydrolase, EC 3.2.1.30) was extracted from malted barley and purified. The partially purified preparation was free from α-and β-glucosidase, α- and β-galactosidase, α-mannosidase and β-mannosidase. This preparation was free from α-mannosidase only after affinity chromatography with p-amino-N-acetyl-β-D-glucosaminidine coupled to Sepharose. The enzyme was active between pH 3 and 6.5 and had a pH optimum at pH 5. A MW of 92000 was obtained by sodium dodecyl sulfate-acrylamide gel electrophoresis and a sedimentation coefficient of 4.65 was obtained from sedimentation velocity experiments. β-N-Acetylaminoglucohydrolase had a K_m of 2.5 × 10^?4 M using the p-nitrophenyl N-acetyl β-D-glucosaminidine as the substrate.     

Generation of α-amylase in germinating Hordeum distichon

The scutellar tissue of germinating barley synthesises significant amounts of a-amylase. The endogenous level of sugars probably limits the initial formation of α-amylase mainly by repressing the supply of gibberellins to the aleurone layer.     

N-feruloylglycyl-l-phenylalanine: A sequence in barley proteins

N-Feruloylglycyl-l-phenylalanine was obtained from barley globulins by partial hydrolysis with 4 N HCl. It was isolated by means of preparative and ‘multiple elimination’ TLC (METC) and further identified by TLC comparison with a synthetic sample. Additional proof for its identity was obtained by UV, fluorescence and IR spectroscopy and by the action of carboxypeptidase A. The possible role of N-feruloylglycine as a starter in protein biosynthesis in the barley seed is discussed.     

Comparison of cytoplasmic ribosomal proteins of gateway barley and its mutant

The proteins of the cytoplasmic ribosomes isolated from dry embryos of Gateway barley and its virescens mutant were compared by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). The monosomes of both the lines gave similar patterns with 60 basic proteins. Upon dissociation of the monosomes, for the mutant, the basic proteins of the large subunits migrated more slowly than those of the normal and lacked three proteins but had three additional spots. Also, the proteins of the small subunits differed. The mutant lacked three of the proteins present in the normal but had three additional spots. Therefore, the large and small subunits contained a total of 34 and 41 basic proteins, respectively, in both the lines. There were several spots with identical electrophoretic mobilities in the small and large subunits of these two lines.     

Effect of carnitine on greening barley leaves

Carnitine increases chlorophyll production in greening barley leaves. [Methyl-¹⁴C]carnitine fed to greening leaves was not utilized as a carbon sou     

Cell specialization within the parenchymatous bundle sheath of barley

Abstract. Structural and physiological aspects of the parenchymatous bundle sheath (PBS) were studied in cultivars of Hordeum distichum L. The PBS of intermediate, lateral and midrib veins consisted of a single layer of cells closely appressed to the mestome sheath. These cells were large, vacuolate and approximately cylindrical in shape, extending parallel to the vein. Mean PBS cell volume was 4 × 10⁻⁵mm³ compared to 1.23 × 10⁻⁵mm³ for mesophyll cells. Transverse sections revealed three cell types within the PBS, cells with small chloroplasts (S-type), cells with large chloroplasts (L-type) and structural cells. The majority of cells were S-type, containing chloroplasts of approximately a third of the volume of mesophyll chloroplasts; they were able to reduce tetranitro blue-tetrazolium and synthesize starch. Structural cells interrupted the phloem and xylem are of the sheath in lateral veins and the midrib, whilst between one and four PBS cells within the phloem are of each vein type contained chloroplasts similar in volume and starch content to those of the mesophyll. Only these L-type cells contained noticeable starch grains at the end of an 8-h dark period, a further 4 h darkness being required for complete mobilization of starch. Starch deposition within S-type and structural cells was detectable after 4 h illumination but was only appreciable in leaves excised from the plant and illuminated for 9–12 h. The role of S-type PBS cells in assimilate transport is discussed in relation to these findings.     

Tissue localization of phytochrome in dark-grown barley leaves

Phytochrome was spectrophotometrically determined to be differentially concentrated among separated tissues of dark-grown, norflurazon-treated barley l     

N-terminal amino acid sequence of C hordein

The C hordein (prolamin storage protein) fraction of barley endosperm has been purified and the N-terminal sequence of amino acids determined for 30 residues. No sequence was obtained for the B hordein fraction because the N-terminus was blocked.     

Stereochemistry of the reaction catalysed by glutamic acid decarboxylase from a higher plant (Hordeum vulgare)

The decarboxylation of (2S)-glutamic acid to yield γ-aminobutyric acid catalysed by L-glutamic acid decarboxylase (EC 4.1.1.15) from Hordeum vulgare proceeds with net retention. The result is interpreted in terms of a single progenitor hypothesis of the pyridoxal phosphate enzymes and confirms that not only bacteria and animals but also plant decarboxylases catalyse the biosynthesis of biogenic amines from amino acids with net retention.     

Metabolism of ent-kaurenol-[17-14C], ent-kaurenal-[17-14C] and ent-kaurenoic acid-[17-14C] by germinating Hordeum distichon grains

Subcellular fractions from germinated barley embryos, chloroplast preparations and whole germinating barley grains are able to carry out the conversions ent-kaurenol → ent-kaurenal → ent-kaurenoic acid → ent-hydroxykaurenoic acid, the initial steps of the biosynthetic pathway to gibberellins. Whole grains, and chloroplasts to a slight extent, incorporate radioactivity from ent-kaurenol-[17-¹⁴C] and ent-kaurenoic acid-[17-¹⁴C] into materials with similar but distinct properties from the gibberellins GA₁, GA₃, GA₄ and GA₇.     

Partial purification and properties of nuclease 1 from barley malt

A sugar-unspecific nuclease has been purified 260-fold from barley malt diastase. The enzyme, a glycoprotein of 37 000 MW, is highly active on single-stranded polynucleotides at pH 5–6. The nuclease is inhibited by several adenine nucleotides, and it binds weakly to NADP-agarose and ATP-agarose.