Purification and partial characterization of a second cysteine proteinase inhibitor from ungerminated barley (Hordeum vulgare L.). 2000

B L Jones, and L A Marinac
Cereal Crops Research Unit, Agricultural Research Service, U.S. Department of Agriculture, Madison, Wisconsin 53705, USA. bljones@facstaff.wisc.edu

It was previously shown that ungerminated barley contains inhibitors that suppress the activities of green malt cysteine proteinases. This paper reports the purification and partial characterization of a second barley cysteine endoproteinase inhibitor, a protein called lipid transfer protein 2 (LTP2). The chromatographically purified inhibitor had a molecular mass of 7112. The amino acid composition and sequence data of the purified inhibitor indicated that it was a protein whose gene, but not the protein itself, was isolated earlier from barley aleurone tissue. The purified protein inhibited the activities of electrophoretically separated green malt cysteine proteinases but not the activities of the serine- or metalloproteinases. The purified LTP2 inhibited the same proteases as the LTP1 that was characterized previously but was present in the mature seed in much smaller amounts. Neither LTP1 nor LTP2 has been proven to transport lipids in vivo, and it seems possible that both serve to keep cysteine endoproteinases that are synthesized during barley seed development inactive until the plant needs them. The small amount of LTP2 in the seed made it impossible to determine whether it, like LTP1, is involved in beer foam formation. Because of its proteinase-inhibiting ability and its resistance to heat inactivation, some of the LTP2 may persist in beer.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010940 Plant Proteins Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. Plant Protein,Protein, Plant,Proteins, Plant
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001467 Hordeum A plant genus of the family POACEAE. The EDIBLE GRAIN, barley, is widely used as food. Barley,Hordeum vulgare
D015853 Cysteine Proteinase Inhibitors Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES. Acid Cysteine Proteinase Inhibitor,Cysteine Protease Inhibitor,Cysteine Protease Inhibitors,Cysteine Proteinase Antagonist,Cysteine Proteinase Antagonists,Cysteine Proteinase Inhibitor,Cysteine Proteinase Inhibitors, Endogenous,Cysteine Proteinase Inhibitors, Exogenous,alpha-Cysteine Protease Inhibitor,Acid Cysteine Proteinase Inhibitors,alpha-Cysteine Protease Inhibitors,Antagonist, Cysteine Proteinase,Antagonists, Cysteine Proteinase,Inhibitor, Cysteine Protease,Inhibitor, Cysteine Proteinase,Inhibitor, alpha-Cysteine Protease,Inhibitors, Cysteine Protease,Inhibitors, Cysteine Proteinase,Inhibitors, alpha-Cysteine Protease,Protease Inhibitor, Cysteine,Protease Inhibitor, alpha-Cysteine,Protease Inhibitors, Cysteine,Protease Inhibitors, alpha-Cysteine,Proteinase Antagonist, Cysteine,Proteinase Antagonists, Cysteine,Proteinase Inhibitor, Cysteine,Proteinase Inhibitors, Cysteine,alpha Cysteine Protease Inhibitor,alpha Cysteine Protease Inhibitors
D050556 Fatty Acid-Binding Proteins Intracellular proteins that reversibly bind hydrophobic ligands including: saturated and unsaturated FATTY ACIDS; EICOSANOIDS; and RETINOIDS. They are considered a highly conserved and ubiquitously expressed family of proteins that may play a role in the metabolism of LIPIDS. Fatty Acid-Binding Protein,Adipocyte Lipid Binding Protein,Adipocyte-Specific Fatty Acid-Binding Protein,Brain-Type Fatty Acid-Binding Protein,Cytosolic Lipid-Binding Proteins,Fatty Acid-Binding Protein, Cardiac Myocyte,Fatty Acid-Binding Protein, Myocardial,Fatty Acid-Binding Proteins, Adipocyte-Specific,Fatty Acid-Binding Proteins, Brain-Specific,Fatty Acid-Binding Proteins, Cytosolic-Specific,Fatty Acid-Binding Proteins, Intestinal-Specific,Fatty Acid-Binding Proteins, Liver-Specific,Fatty Acid-Binding Proteins, Myocardial-Specific,Fatty Acid-Binding Proteins, Plasma-Membrane Specific,Intestinal Fatty Acid-Binding Protein,Liver Fatty Acid-Binding Protein,Myocardial Fatty Acid-Binding Protein,Plasma Membrane Fatty Acid-Binding Protein,Acid-Binding Protein, Fatty,Adipocyte Specific Fatty Acid Binding Protein,Brain Type Fatty Acid Binding Protein,Cytosolic Lipid Binding Proteins,Fatty Acid Binding Protein,Fatty Acid Binding Protein, Cardiac Myocyte,Fatty Acid Binding Protein, Myocardial,Fatty Acid Binding Proteins,Fatty Acid Binding Proteins, Adipocyte Specific,Fatty Acid Binding Proteins, Brain Specific,Fatty Acid Binding Proteins, Cytosolic Specific,Fatty Acid Binding Proteins, Intestinal Specific,Fatty Acid Binding Proteins, Liver Specific,Fatty Acid Binding Proteins, Myocardial Specific,Fatty Acid Binding Proteins, Plasma Membrane Specific,Intestinal Fatty Acid Binding Protein,Lipid-Binding Proteins, Cytosolic,Liver Fatty Acid Binding Protein,Myocardial Fatty Acid Binding Protein,Plasma Membrane Fatty Acid Binding Protein,Protein, Fatty Acid-Binding
D018525 Germination The initial stages of the growth of SEEDS into a SEEDLINGS. The embryonic shoot (plumule) and embryonic PLANT ROOTS (radicle) emerge and grow upwards and downwards respectively. Food reserves for germination come from endosperm tissue within the seed and/or from the seed leaves (COTYLEDON). (Concise Dictionary of Biology, 1990) Germinations

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