The Experts below are selected from a list of 51 Experts worldwide ranked by ideXlab platform
Friedrich Lottspeich - One of the best experts on this subject based on the ideXlab platform.
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high molecular weight Aspartic Endopeptidase generates a coronaro constrictory peptide from the β chain of hemoglobin
FEBS Letters, 1993Co-Authors: Nina Barkhudaryan, Josef Kellermann, A A Galoyan, Friedrich LottspeichAbstract:Studying the influence of brain cathepsin D (EC 3.4.23.5) and high molecular weight (HMW) Aspartic Endopeptidase (EC 3.4.23.-) on the processing of hypothalamic calmodulin-binding coronaro-constrictory peptide factors from the beta-chain of globin it was found that only HMW Aspartic Endopeptidase generates the fragment 31-40 of the beta-chain of bovine hemoglobin (Hb) by cleavage of the Leu30-Leu31 and Phe40-Phe41 bonds. Digestion of the beta-chain of globin was performed at 37 degrees C at an enzyme/substrate ratio of 1:80 at pH 3.5 using different times of incubation (from 4 h to 10 h). The resulting peptides were separated by reversed-phase high-performance liquid chromatography (HPLC) and then identified by amino acid analysis and Edman degradation. The differences in specificity and activity of these two brain Aspartic proteinases could be explained by their different structural features. Our finding provides evidence for a different biological function of these two enzymes. Data obtained give us reason to suppose that HMW Aspartic proteinase probably can participate in the processing of the coronaro-constrictory peptide in vivo by limited proteolysis of Hb or Hb-like protein.
Nina Barkhudaryan - One of the best experts on this subject based on the ideXlab platform.
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high molecular weight Aspartic Endopeptidase generates a coronaro constrictory peptide from the β chain of hemoglobin
FEBS Letters, 1993Co-Authors: Nina Barkhudaryan, Josef Kellermann, A A Galoyan, Friedrich LottspeichAbstract:Studying the influence of brain cathepsin D (EC 3.4.23.5) and high molecular weight (HMW) Aspartic Endopeptidase (EC 3.4.23.-) on the processing of hypothalamic calmodulin-binding coronaro-constrictory peptide factors from the beta-chain of globin it was found that only HMW Aspartic Endopeptidase generates the fragment 31-40 of the beta-chain of bovine hemoglobin (Hb) by cleavage of the Leu30-Leu31 and Phe40-Phe41 bonds. Digestion of the beta-chain of globin was performed at 37 degrees C at an enzyme/substrate ratio of 1:80 at pH 3.5 using different times of incubation (from 4 h to 10 h). The resulting peptides were separated by reversed-phase high-performance liquid chromatography (HPLC) and then identified by amino acid analysis and Edman degradation. The differences in specificity and activity of these two brain Aspartic proteinases could be explained by their different structural features. Our finding provides evidence for a different biological function of these two enzymes. Data obtained give us reason to suppose that HMW Aspartic proteinase probably can participate in the processing of the coronaro-constrictory peptide in vivo by limited proteolysis of Hb or Hb-like protein.
Renate Kaiser-alexnat - One of the best experts on this subject based on the ideXlab platform.
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Protease activities in the midgut of Western corn rootworm (Diabrotica virgifera virgifera LeConte).
Journal of invertebrate pathology, 2009Co-Authors: Renate Kaiser-alexnatAbstract:The Western corn rootworm is one of the most economically important pests in corn. One possibility for controlling this pest is the cultivation of transgenic corn expressing Bacillus thuringiensis (Bt) toxins, such as Cry3A, Cry34Ab1/Cry35Ab1, and Cry3Bb1. However, widespread cultivation of the resulting Bt corn may result in the development of resistant pest populations. The Bt toxins are processed by proteases in the midgut of susceptible insects. Thus, protease activity studies were conducted using the midgut juice (pH 5.75) from third instars larvae of the susceptible Western corn rootworm. As a result, the activities of the serine Endopeptidases trypsin, chymotrypsin, elastase, cathepsin G, plasmin, and thrombin; the cysteine Endopeptidases cathepsin L, papain, cathepsin B, and cathepsin H; the Aspartic Endopeptidase pepsin; the metallo Endopeptidase saccharolysin; the exopeptidase aminopeptidase, and the omegapeptidase acylaminoacylpeptidase were detected. These results are of basic interest but also lead to reference systems for the identification of protease-mediated resistance mechanisms in potentially resistant individuals.
A A Galoyan - One of the best experts on this subject based on the ideXlab platform.
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high molecular weight Aspartic Endopeptidase generates a coronaro constrictory peptide from the β chain of hemoglobin
FEBS Letters, 1993Co-Authors: Nina Barkhudaryan, Josef Kellermann, A A Galoyan, Friedrich LottspeichAbstract:Studying the influence of brain cathepsin D (EC 3.4.23.5) and high molecular weight (HMW) Aspartic Endopeptidase (EC 3.4.23.-) on the processing of hypothalamic calmodulin-binding coronaro-constrictory peptide factors from the beta-chain of globin it was found that only HMW Aspartic Endopeptidase generates the fragment 31-40 of the beta-chain of bovine hemoglobin (Hb) by cleavage of the Leu30-Leu31 and Phe40-Phe41 bonds. Digestion of the beta-chain of globin was performed at 37 degrees C at an enzyme/substrate ratio of 1:80 at pH 3.5 using different times of incubation (from 4 h to 10 h). The resulting peptides were separated by reversed-phase high-performance liquid chromatography (HPLC) and then identified by amino acid analysis and Edman degradation. The differences in specificity and activity of these two brain Aspartic proteinases could be explained by their different structural features. Our finding provides evidence for a different biological function of these two enzymes. Data obtained give us reason to suppose that HMW Aspartic proteinase probably can participate in the processing of the coronaro-constrictory peptide in vivo by limited proteolysis of Hb or Hb-like protein.
Josef Kellermann - One of the best experts on this subject based on the ideXlab platform.
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high molecular weight Aspartic Endopeptidase generates a coronaro constrictory peptide from the β chain of hemoglobin
FEBS Letters, 1993Co-Authors: Nina Barkhudaryan, Josef Kellermann, A A Galoyan, Friedrich LottspeichAbstract:Studying the influence of brain cathepsin D (EC 3.4.23.5) and high molecular weight (HMW) Aspartic Endopeptidase (EC 3.4.23.-) on the processing of hypothalamic calmodulin-binding coronaro-constrictory peptide factors from the beta-chain of globin it was found that only HMW Aspartic Endopeptidase generates the fragment 31-40 of the beta-chain of bovine hemoglobin (Hb) by cleavage of the Leu30-Leu31 and Phe40-Phe41 bonds. Digestion of the beta-chain of globin was performed at 37 degrees C at an enzyme/substrate ratio of 1:80 at pH 3.5 using different times of incubation (from 4 h to 10 h). The resulting peptides were separated by reversed-phase high-performance liquid chromatography (HPLC) and then identified by amino acid analysis and Edman degradation. The differences in specificity and activity of these two brain Aspartic proteinases could be explained by their different structural features. Our finding provides evidence for a different biological function of these two enzymes. Data obtained give us reason to suppose that HMW Aspartic proteinase probably can participate in the processing of the coronaro-constrictory peptide in vivo by limited proteolysis of Hb or Hb-like protein.