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Showing 25 to 36 of 753 entries
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Succinylation of the amino group of isoleucine 16 in delta-chymotrypsin with retention of activity.

FEBS letters

Blair TT, Marini MA, Agarwal SP, Martin CJ.
PMID: 11945725
FEBS Lett. 1971 Apr;14(2):86-88. doi: 10.1016/0014-5793(71)80106-0.

No abstract available.

Cite
Blair TT, Marini MA, Agarwal SP, et al. Succinylation of the amino group of isoleucine 16 in delta-chymotrypsin with retention of activity. FEBS Lett. 1971;14(2):86-88doi: 10.1016/0014-5793(71)80106-0.
Blair, T. T., Marini, M. A., Agarwal, S. P., & Martin, C. J. (1971). Succinylation of the amino group of isoleucine 16 in delta-chymotrypsin with retention of activity. FEBS letters, 14(2), 86-88. https://doi.org/10.1016/0014-5793(71)80106-0
Blair, T T., et al. "Succinylation of the amino group of isoleucine 16 in delta-chymotrypsin with retention of activity." FEBS letters vol. 14,2 (1971): 86-88. doi: https://doi.org/10.1016/0014-5793(71)80106-0
Blair TT, Marini MA, Agarwal SP, Martin CJ. Succinylation of the amino group of isoleucine 16 in delta-chymotrypsin with retention of activity. FEBS Lett. 1971 Apr;14(2):86-88. doi: 10.1016/0014-5793(71)80106-0. PMID: 11945725.
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Long-term stability of alpha-1-antichymotrypsin complexed form of prostate specific antigen.

Prostate cancer and prostatic diseases

Brawer MK, Ferreri LF, Bankson DD.
PMID: 12497096
Prostate Cancer Prostatic Dis. 2000 Nov;3(3):191-194. doi: 10.1038/sj.pcan.4500419.

PSA complexed with alpha-1-anti-chymotrypsin (cPSA trade mark ) is the moiety in greatest proportion in the serum of men with prostate cancer (CAP). The performance of this analyte has been established primarily in retrospective archival serum. Studies indicate cPSA...

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Brawer MK, Ferreri LF, Bankson DD. Long-term stability of alpha-1-antichymotrypsin complexed form of prostate specific antigen. Prostate Cancer Prostatic Dis. 2000;3(3):191-194doi: 10.1038/sj.pcan.4500419.
Brawer, M. K., Ferreri, L. F., & Bankson, D. D. (2000). Long-term stability of alpha-1-antichymotrypsin complexed form of prostate specific antigen. Prostate cancer and prostatic diseases, 3(3), 191-194. https://doi.org/10.1038/sj.pcan.4500419
Brawer, M K, et al. "Long-term stability of alpha-1-antichymotrypsin complexed form of prostate specific antigen." Prostate cancer and prostatic diseases vol. 3,3 (2000): 191-194. doi: https://doi.org/10.1038/sj.pcan.4500419
Brawer MK, Ferreri LF, Bankson DD. Long-term stability of alpha-1-antichymotrypsin complexed form of prostate specific antigen. Prostate Cancer Prostatic Dis. 2000 Nov;3(3):191-194. doi: 10.1038/sj.pcan.4500419. PMID: 12497096.
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Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds.

Journal of biomedical science

Chow LP, Kamo M, Lin JY, Wang SH, Ueno Y, Tsugita A.
PMID: 11725098
J Biomed Sci. 1996 May-Jun;3(3):178-186. doi: 10.1007/BF02253098.

In this study, we sequenced a new type I ribosome-inactivating protein, trichoanguina, from the seeds of Trichosanthes anguina (snake gourd). Trichoanguina is a basic glycoprotein having an apparent molecular mass of 35.0 kD and possessing strong ribosome-inactivating activity. Trichoanguina...

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Chow LP, Kamo M, Lin JY, et al. Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. J Biomed Sci. 1996;3(3):178-186doi: 10.1007/BF02253098.
Chow, L. P., Kamo, M., Lin, J. Y., Wang, S. H., Ueno, Y., & Tsugita, A. (1996). Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. Journal of biomedical science, 3(3), 178-186. https://doi.org/10.1007/BF02253098
Chow, L.-P., et al. "Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds." Journal of biomedical science vol. 3,3 (1996): 178-186. doi: https://doi.org/10.1007/BF02253098
Chow LP, Kamo M, Lin JY, Wang SH, Ueno Y, Tsugita A. Amino Acid Sequence of Trichoanguina, a Ribosomal-Inactivating Protein from Trichosanthes anguinea Seeds. J Biomed Sci. 1996 May-Jun;3(3):178-186. doi: 10.1007/BF02253098. PMID: 11725098.
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The catalytic activity of the inactive conformation of delta-chymotrypsin.

FEBS letters

Fersht AR.
PMID: 11946933
FEBS Lett. 1973 Feb 01;29(3):283-285. doi: 10.1016/0014-5793(73)80039-0.

No abstract available.

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Fersht AR. The catalytic activity of the inactive conformation of delta-chymotrypsin. FEBS Lett. 1973;29(3):283-285doi: 10.1016/0014-5793(73)80039-0.
Fersht, A. R. (1973). The catalytic activity of the inactive conformation of delta-chymotrypsin. FEBS letters, 29(3), 283-285. https://doi.org/10.1016/0014-5793(73)80039-0
Fersht, A R.. "The catalytic activity of the inactive conformation of delta-chymotrypsin." FEBS letters vol. 29,3 (1973): 283-285. doi: https://doi.org/10.1016/0014-5793(73)80039-0
Fersht AR. The catalytic activity of the inactive conformation of delta-chymotrypsin. FEBS Lett. 1973 Feb 01;29(3):283-285. doi: 10.1016/0014-5793(73)80039-0. PMID: 11946933.
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Pancreatic Enzyme Supplementation Therapy.

Current treatment options in gastroenterology

Keller J, Layer P.
PMID: 12954143
Curr Treat Options Gastroenterol. 2003 Oct;6(5):369-374. doi: 10.1007/s11938-003-0039-0.

Effective treatment of malabsorption due to severe pancreatic exocrine insufficiency requires delivery of sufficient enzymatic activity into the duodenal lumen simultaneously with meal nutrients. To achieve this, modern therapeutic concepts recommend administration of 25,000 to 40,000 units of lipase...

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Keller J, Layer P. Pancreatic Enzyme Supplementation Therapy. Curr Treat Options Gastroenterol. 2003;6(5):369-374doi: 10.1007/s11938-003-0039-0.
Keller, J., & Layer, P. (2003). Pancreatic Enzyme Supplementation Therapy. Current treatment options in gastroenterology, 6(5), 369-374. https://doi.org/10.1007/s11938-003-0039-0
Keller, Jutta, and Layer, Peter. "Pancreatic Enzyme Supplementation Therapy." Current treatment options in gastroenterology vol. 6,5 (2003): 369-374. doi: https://doi.org/10.1007/s11938-003-0039-0
Keller J, Layer P. Pancreatic Enzyme Supplementation Therapy. Curr Treat Options Gastroenterol. 2003 Oct;6(5):369-374. doi: 10.1007/s11938-003-0039-0. PMID: 12954143.
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Light-initiated enzymic activity caused by photostereoisomerization of cis-4-nitrocinnamoyl-alpha-chymotrypsin.

FEBS letters

Varfolomeyev SD, Klibanov AM, Martinek K, Berezin IV.
PMID: 11945826
FEBS Lett. 1971 Jun 10;15(2):118-120. doi: 10.1016/0014-5793(71)80036-4.

No abstract available.

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Varfolomeyev SD, Klibanov AM, Martinek K, et al. Light-initiated enzymic activity caused by photostereoisomerization of cis-4-nitrocinnamoyl-alpha-chymotrypsin. FEBS Lett. 1971;15(2):118-120doi: 10.1016/0014-5793(71)80036-4.
Varfolomeyev, S. D., Klibanov, A. M., Martinek, K., & Berezin, I. V. (1971). Light-initiated enzymic activity caused by photostereoisomerization of cis-4-nitrocinnamoyl-alpha-chymotrypsin. FEBS letters, 15(2), 118-120. https://doi.org/10.1016/0014-5793(71)80036-4
Varfolomeyev, S D., et al. "Light-initiated enzymic activity caused by photostereoisomerization of cis-4-nitrocinnamoyl-alpha-chymotrypsin." FEBS letters vol. 15,2 (1971): 118-120. doi: https://doi.org/10.1016/0014-5793(71)80036-4
Varfolomeyev SD, Klibanov AM, Martinek K, Berezin IV. Light-initiated enzymic activity caused by photostereoisomerization of cis-4-nitrocinnamoyl-alpha-chymotrypsin. FEBS Lett. 1971 Jun 10;15(2):118-120. doi: 10.1016/0014-5793(71)80036-4. PMID: 11945826.
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Binding-catalysis relationship in alpha-chymotrypsin action as revealed from reversible inhibition study of phenylalkylboronic acids.

FEBS letters

Antonov VK, Ivanina TV, Ivanova AG, Berezin IV, Levashov AV, Martinek K.
PMID: 11946376
FEBS Lett. 1972 Jan 15;20(1):37-40. doi: 10.1016/0014-5793(72)80011-5.

No abstract available.

Cite
Antonov VK, Ivanina TV, Ivanova AG, et al. Binding-catalysis relationship in alpha-chymotrypsin action as revealed from reversible inhibition study of phenylalkylboronic acids. FEBS Lett. 1972;20(1):37-40doi: 10.1016/0014-5793(72)80011-5.
Antonov, V. K., Ivanina, T. V., Ivanova, A. G., Berezin, I. V., Levashov, A. V., & Martinek, K. (1972). Binding-catalysis relationship in alpha-chymotrypsin action as revealed from reversible inhibition study of phenylalkylboronic acids. FEBS letters, 20(1), 37-40. https://doi.org/10.1016/0014-5793(72)80011-5
Antonov, V K., et al. "Binding-catalysis relationship in alpha-chymotrypsin action as revealed from reversible inhibition study of phenylalkylboronic acids." FEBS letters vol. 20,1 (1972): 37-40. doi: https://doi.org/10.1016/0014-5793(72)80011-5
Antonov VK, Ivanina TV, Ivanova AG, Berezin IV, Levashov AV, Martinek K. Binding-catalysis relationship in alpha-chymotrypsin action as revealed from reversible inhibition study of phenylalkylboronic acids. FEBS Lett. 1972 Jan 15;20(1):37-40. doi: 10.1016/0014-5793(72)80011-5. PMID: 11946376.
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Limited proteolysis of NACP/alpha-synuclein.

Journal of Alzheimer's disease : JAD

Hossain S, Alim A, Takeda K, Kaji H, Shinoda T, Uéda K.
PMID: 12214024
J Alzheimers Dis. 2001 Dec;3(6):577-584. doi: 10.3233/jad-2001-3608.

The NAC region of NACP/alpha-synuclein is a secondary component of Alzheimer's disease amyloid. alpha-Synuclein is a major component of Lewy bodies, a typical neuropathological feature of Parkinson's disease. However, the physiological role and deposition mechanisms of alpha-synuclein are unknown....

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Hossain S, Alim A, Takeda K, et al. Limited proteolysis of NACP/alpha-synuclein. J Alzheimers Dis. 2001;3(6):577-584doi: 10.3233/jad-2001-3608.
Hossain, S., Alim, A., Takeda, K., Kaji, H., Shinoda, T., & Uéda, K. (2001). Limited proteolysis of NACP/alpha-synuclein. Journal of Alzheimer's disease : JAD, 3(6), 577-584. https://doi.org/10.3233/jad-2001-3608
Hossain, Shahanara, et al. "Limited proteolysis of NACP/alpha-synuclein." Journal of Alzheimer's disease : JAD vol. 3,6 (2001): 577-584. doi: https://doi.org/10.3233/jad-2001-3608
Hossain S, Alim A, Takeda K, Kaji H, Shinoda T, Uéda K. Limited proteolysis of NACP/alpha-synuclein. J Alzheimers Dis. 2001 Dec;3(6):577-584. doi: 10.3233/jad-2001-3608. PMID: 12214024.
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[No title available]

FEBS letters

Kleine R, Schubert J.
PMID: 11946635
FEBS Lett. 1972 May 15;22(3):352-355. doi: 10.1016/0014-5793(72)80268-0.

The high molecular weight arylamidase-alkaline phosphatase-complex from rat kidney microsomes [1] was carefully dissociated by means of treatment with several hydrolytic enzymes or by acidification. Trypsin, chymotrypsin and pronase cause a selective solubilization of the enzymes discernible at their...

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Kleine R, Schubert J. Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren. . FEBS Lett. 1972;22(3):352-355doi: 10.1016/0014-5793(72)80268-0.
Kleine, R., & Schubert, J. (1972). Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren. . FEBS letters, 22(3), 352-355. https://doi.org/10.1016/0014-5793(72)80268-0
Kleine, R, and Schubert, J. "Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren." . FEBS letters vol. 22,3 (1972): 352-355. doi: https://doi.org/10.1016/0014-5793(72)80268-0
Kleine R, Schubert J. Dissoziation des mikrosomalen arylamidase-alkalischen phosphatase-komplexes aus rattennieren. . FEBS Lett. 1972 May 15;22(3):352-355. doi: 10.1016/0014-5793(72)80268-0. French. PMID: 11946635.
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Alpha 1-antichymotrypsin inhibits chymotrypsin-induced apoptosis in rat hepatoma cells.

Apoptosis : an international journal on programmed cell death

Emoto T, Nakamura K, Nagasaka Y, Numa F, Suminami Y, Kato H.
PMID: 14646496
Apoptosis. 1998;3(3):155-60. doi: 10.1023/a:1009694621397.

Increased serum levels of alpha1-antichymotrypsin (alpha 1ACT) are observed in some cancer patients, especially those with hepatocellular carcinoma. A possible role of alpha 1ACT in tumour growth has been suggested, but this remains uncertain. We have demonstrated that alpha...

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Emoto T, Nakamura K, Nagasaka Y, et al. Alpha 1-antichymotrypsin inhibits chymotrypsin-induced apoptosis in rat hepatoma cells. Apoptosis. 1998;3(3):155-60doi: 10.1023/a:1009694621397.
Emoto, T., Nakamura, K., Nagasaka, Y., Numa, F., Suminami, Y., & Kato, H. (1998). Alpha 1-antichymotrypsin inhibits chymotrypsin-induced apoptosis in rat hepatoma cells. Apoptosis : an international journal on programmed cell death, 3(3), 155-60. https://doi.org/10.1023/a:1009694621397
Emoto, T, et al. "Alpha 1-antichymotrypsin inhibits chymotrypsin-induced apoptosis in rat hepatoma cells." Apoptosis : an international journal on programmed cell death vol. 3,3 (1998): 155-60. doi: https://doi.org/10.1023/a:1009694621397
Emoto T, Nakamura K, Nagasaka Y, Numa F, Suminami Y, Kato H. Alpha 1-antichymotrypsin inhibits chymotrypsin-induced apoptosis in rat hepatoma cells. Apoptosis. 1998;3(3):155-60. doi: 10.1023/a:1009694621397. PMID: 14646496.
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The reactivity of carboxyl groups in chymotrypsinogen.

FEBS letters

Abita JP, Maroux S, Delaage M, Lazdunski M.
PMID: 11947183
FEBS Lett. 1969 Aug;4(3):203-206. doi: 10.1016/0014-5793(69)80235-8.

No abstract available.

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Abita JP, Maroux S, Delaage M, et al. The reactivity of carboxyl groups in chymotrypsinogen. FEBS Lett. 1969;4(3):203-206doi: 10.1016/0014-5793(69)80235-8.
Abita, J. P., Maroux, S., Delaage, M., & Lazdunski, M. (1969). The reactivity of carboxyl groups in chymotrypsinogen. FEBS letters, 4(3), 203-206. https://doi.org/10.1016/0014-5793(69)80235-8
Abita, J P., et al. "The reactivity of carboxyl groups in chymotrypsinogen." FEBS letters vol. 4,3 (1969): 203-206. doi: https://doi.org/10.1016/0014-5793(69)80235-8
Abita JP, Maroux S, Delaage M, Lazdunski M. The reactivity of carboxyl groups in chymotrypsinogen. FEBS Lett. 1969 Aug;4(3):203-206. doi: 10.1016/0014-5793(69)80235-8. PMID: 11947183.
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On the mechanism of the alpha-chymotrypsin-catalysed hydrolysis of 4-cis-benzylidene-2-phenyloxazolin-5-one: Evidence for covalent non-productive binding.

FEBS letters

Brocklehurst K.
PMID: 11947240
FEBS Lett. 1969 Sep;5(1):63-67. doi: 10.1016/0014-5793(69)80294-2.

No abstract available.

Cite
Brocklehurst K. On the mechanism of the alpha-chymotrypsin-catalysed hydrolysis of 4-cis-benzylidene-2-phenyloxazolin-5-one: Evidence for covalent non-productive binding. FEBS Lett. 1969;5(1):63-67doi: 10.1016/0014-5793(69)80294-2.
Brocklehurst, K. (1969). On the mechanism of the alpha-chymotrypsin-catalysed hydrolysis of 4-cis-benzylidene-2-phenyloxazolin-5-one: Evidence for covalent non-productive binding. FEBS letters, 5(1), 63-67. https://doi.org/10.1016/0014-5793(69)80294-2
Brocklehurst, K. "On the mechanism of the alpha-chymotrypsin-catalysed hydrolysis of 4-cis-benzylidene-2-phenyloxazolin-5-one: Evidence for covalent non-productive binding." FEBS letters vol. 5,1 (1969): 63-67. doi: https://doi.org/10.1016/0014-5793(69)80294-2
Brocklehurst K. On the mechanism of the alpha-chymotrypsin-catalysed hydrolysis of 4-cis-benzylidene-2-phenyloxazolin-5-one: Evidence for covalent non-productive binding. FEBS Lett. 1969 Sep;5(1):63-67. doi: 10.1016/0014-5793(69)80294-2. PMID: 11947240.
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Showing 25 to 36 of 753 entries