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Showing 1 to 8 of 8 entries
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Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris).

Planta

Pusztai A, Duncan I.
PMID: 24493138
Planta. 1971 Dec;96(4):317-25. doi: 10.1007/BF00386946.

Hydrolytic activity towards synthetic substrates and denatured proteins was measured in the extracts of the seeds of kidney bean at various stages of germination up to 16 days.Of the peptide hydrolases, chymotrypsin-type activity was stable for the first 7...

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Pusztai A, Duncan I. Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris). Planta. 1971;96(4):317-25doi: 10.1007/BF00386946.
Pusztai, A., & Duncan, I. (1971). Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris). Planta, 96(4), 317-25. https://doi.org/10.1007/BF00386946
Pusztai, A, and Duncan, I. "Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris)." Planta vol. 96,4 (1971): 317-25. doi: https://doi.org/10.1007/BF00386946
Pusztai A, Duncan I. Changes in proteolytic enzyme activities and transformation of nitrogenous compounds in the germinating seeds of kidney bean (Phaseolus vulgaris). Planta. 1971 Dec;96(4):317-25. doi: 10.1007/BF00386946. PMID: 24493138.
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Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness.

BMC oral health

Yamamoto K, Hiraishi M, Haneoka M, Fujinaka H, Yano Y.
PMID: 34930236
BMC Oral Health. 2021 Dec 20;21(1):661. doi: 10.1186/s12903-021-02024-x.

BACKGROUND: Oral dryness is a common symptom that may interfere with swallowing, chewing, and taste. The most common reason for oral dryness is hyposalivation. Some individuals experiencing oral dryness do not have hyposalivation, however, and the reverse is also...

Cite
Yamamoto K, Hiraishi M, Haneoka M, et al. Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness. BMC Oral Health. 2021;21(1):661doi: 10.1186/s12903-021-02024-x.
Yamamoto, K., Hiraishi, M., Haneoka, M., Fujinaka, H., & Yano, Y. (2021). Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness. BMC oral health, 21(1), 661. https://doi.org/10.1186/s12903-021-02024-x
Yamamoto, Kenkichi, et al. "Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness." BMC oral health vol. 21,1 (2021): 661. doi: https://doi.org/10.1186/s12903-021-02024-x
Yamamoto K, Hiraishi M, Haneoka M, Fujinaka H, Yano Y. Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness. BMC Oral Health. 2021 Dec 20;21(1):661. doi: 10.1186/s12903-021-02024-x. PMID: 34930236; PMCID: PMC8686663.
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An Undiagnosed Case of Chronic Pancreatitis With Multiple Visceral Arteries Pseudoaneurysm.

Cureus

Anwar MN, Anthony N, Amin QK, Yousafzai ZA, Khalil H.
PMID: 34094751
Cureus. 2021 May 01;13(5):e14789. doi: 10.7759/cureus.14789.

Visceral artery aneurysms, which could be either true or pseudo, are abnormal focal dilations of vessels supplying the abdominal organs. True aneurysms, by definition, suggest dilation of the vessel in response to increased blood flow, ultimately causing a blood-filled...

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Anwar MN, Anthony N, Amin QK, et al. An Undiagnosed Case of Chronic Pancreatitis With Multiple Visceral Arteries Pseudoaneurysm. Cureus. 2021;13(5):e14789doi: 10.7759/cureus.14789.
Anwar, M. N., Anthony, N., Amin, Q. K., Yousafzai, Z. A., & Khalil, H. (2021). An Undiagnosed Case of Chronic Pancreatitis With Multiple Visceral Arteries Pseudoaneurysm. Cureus, 13(5), e14789. https://doi.org/10.7759/cureus.14789
Anwar, Muhammad Naveed, et al. "An Undiagnosed Case of Chronic Pancreatitis With Multiple Visceral Arteries Pseudoaneurysm." Cureus vol. 13,5 (2021): e14789. doi: https://doi.org/10.7759/cureus.14789
Anwar MN, Anthony N, Amin QK, Yousafzai ZA, Khalil H. An Undiagnosed Case of Chronic Pancreatitis With Multiple Visceral Arteries Pseudoaneurysm. Cureus. 2021 May 01;13(5):e14789. doi: 10.7759/cureus.14789. PMID: 34094751; PMCID: PMC8169010.
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In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor.

Plant physiology

Sherrard JH, Kennedy JA, Dalling MJ.
PMID: 16661024
Plant Physiol. 1979 Oct;64(4):640-5. doi: 10.1104/pp.64.4.640.

A nitrate reductase (EC 1.6.6.1)-inactivating factor has been isolated from 8-day-old wheat leaves. The purification schedule involved ammonium sulfate precipitation, Sephadex G-100 filtration, DEAE-cellulose chromatography, and Sephadex G-150 filtration. No accurate assessment could be made as to the degree...

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Sherrard JH, Kennedy JA, Dalling MJ. In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor. Plant Physiol. 1979;64(4):640-5doi: 10.1104/pp.64.4.640.
Sherrard, J. H., Kennedy, J. A., & Dalling, M. J. (1979). In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor. Plant physiology, 64(4), 640-5. https://doi.org/10.1104/pp.64.4.640
Sherrard, J H, et al. "In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor." Plant physiology vol. 64,4 (1979): 640-5. doi: https://doi.org/10.1104/pp.64.4.640
Sherrard JH, Kennedy JA, Dalling MJ. In Vitro Stability of Nitrate Reductase from Wheat Leaves: III. Isolation and Partial Characterization of a Nitrate Reductase-inactivating Factor. Plant Physiol. 1979 Oct;64(4):640-5. doi: 10.1104/pp.64.4.640. PMID: 16661024; PMCID: PMC543152.
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Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves.

Plant physiology

Waters SP, Noble ER, Dalling MJ.
PMID: 16662252
Plant Physiol. 1982 Mar;69(3):575-9. doi: 10.1104/pp.69.3.575.

Protoplasts from 8- to 9-day-old wheat (Triticum aestivum L.) leaves were used to isolate organelles which were examined for their contents of peptide hydrolase enzymes and, in the case of vacuoles, other acid hydrolases. High yields of intact chloroplasts...

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Waters SP, Noble ER, Dalling MJ. Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves. Plant Physiol. 1982;69(3):575-9doi: 10.1104/pp.69.3.575.
Waters, S. P., Noble, E. R., & Dalling, M. J. (1982). Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves. Plant physiology, 69(3), 575-9. https://doi.org/10.1104/pp.69.3.575
Waters, S P, et al. "Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves." Plant physiology vol. 69,3 (1982): 575-9. doi: https://doi.org/10.1104/pp.69.3.575
Waters SP, Noble ER, Dalling MJ. Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves. Plant Physiol. 1982 Mar;69(3):575-9. doi: 10.1104/pp.69.3.575. PMID: 16662252; PMCID: PMC426257.
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Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness.

BMC oral health

Yamamoto K, Hiraishi M, Haneoka M, Fujinaka H, Yano Y.
PMID: 34930236
BMC Oral Health. 2021 Dec 20;21(1):661. doi: 10.1186/s12903-021-02024-x.

BACKGROUND: Oral dryness is a common symptom that may interfere with swallowing, chewing, and taste. The most common reason for oral dryness is hyposalivation. Some individuals experiencing oral dryness do not have hyposalivation, however, and the reverse is also...

Cite
Yamamoto K, Hiraishi M, Haneoka M, et al. Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness. BMC Oral Health. 2021;21(1):661doi: 10.1186/s12903-021-02024-x.
Yamamoto, K., Hiraishi, M., Haneoka, M., Fujinaka, H., & Yano, Y. (2021). Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness. BMC oral health, 21(1), 661. https://doi.org/10.1186/s12903-021-02024-x
Yamamoto, Kenkichi, et al. "Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness." BMC oral health vol. 21,1 (2021): 661. doi: https://doi.org/10.1186/s12903-021-02024-x
Yamamoto K, Hiraishi M, Haneoka M, Fujinaka H, Yano Y. Protease inhibitor concentrations in the saliva of individuals experiencing oral dryness. BMC Oral Health. 2021 Dec 20;21(1):661. doi: 10.1186/s12903-021-02024-x. PMID: 34930236.
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Partial purification and characterization of two Peptide hydrolases from pea seeds.

Plant physiology

Caldwell JB, Sparrow LG.
PMID: 16659571
Plant Physiol. 1976 May;57(5):795-8. doi: 10.1104/pp.57.5.795.

Two peptide hydrolases have been found in pea seeds (Pisum sativum var. Greenfeast) and extensively purified by ion exchange chromatography using benzoyl-dl-arginine-p-nitroanilide as substrate. The enzymes which both have molecular weights of 65,000 can be separated by anion exchange...

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Caldwell JB, Sparrow LG. Partial purification and characterization of two Peptide hydrolases from pea seeds. Plant Physiol. 1976;57(5):795-8doi: 10.1104/pp.57.5.795.
Caldwell, J. B., & Sparrow, L. G. (1976). Partial purification and characterization of two Peptide hydrolases from pea seeds. Plant physiology, 57(5), 795-8. https://doi.org/10.1104/pp.57.5.795
Caldwell, J B, and Sparrow, L G. "Partial purification and characterization of two Peptide hydrolases from pea seeds." Plant physiology vol. 57,5 (1976): 795-8. doi: https://doi.org/10.1104/pp.57.5.795
Caldwell JB, Sparrow LG. Partial purification and characterization of two Peptide hydrolases from pea seeds. Plant Physiol. 1976 May;57(5):795-8. doi: 10.1104/pp.57.5.795. PMID: 16659571; PMCID: PMC542119.
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Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature.

Journal of food protection

Chaia AP, de Ruiz Holgado AP, Oliver G.
PMID: 31018387
J Food Prot. 1990 Mar;53(3):237-240. doi: 10.4315/0362-028X-53.3.237.

A comparative study of the activity of peptidases belonging to the four classic propionibacteria species cultured in milk was carried out at different values of pH and temperature. Leucine aminopeptidase and proline iminopeptidase showed greater activity in Propionibacterium freudenreichii...

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Chaia AP, de Ruiz Holgado AP, Oliver G. Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature. J Food Prot. 1990;53(3):237-240doi: 10.4315/0362-028X-53.3.237.
Chaia, A. P., de Ruiz Holgado, A. P., & Oliver, G. (1990). Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature. Journal of food protection, 53(3), 237-240. https://doi.org/10.4315/0362-028X-53.3.237
Chaia, Adriana Perez, et al. "Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature." Journal of food protection vol. 53,3 (1990): 237-240. doi: https://doi.org/10.4315/0362-028X-53.3.237
Chaia AP, de Ruiz Holgado AP, Oliver G. Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature. J Food Prot. 1990 Mar;53(3):237-240. doi: 10.4315/0362-028X-53.3.237. PMID: 31018387.
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Showing 1 to 8 of 8 entries