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Showing 1 to 7 of 7 entries
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Globulin-specific Proteolytic Activity in Germinating Pumpkin Seeds as Detected by a Fluorescence Assay Method.

Plant physiology

Spencer PW, Spencer RD.
PMID: 16659002
Plant Physiol. 1974 Dec;54(6):925-30. doi: 10.1104/pp.54.6.925.

The proteolytic activities of alpha-chymotrypsin, trypsin, pepsin, bromelain, and an extract from germinating pumpkin seeds (Cucurbita moschata) were determined by their ability to effect the release of 1-anilino-8-naphthalenesulfonate bound to internal hydrophobic sites in intact protein substrates. Casein, glyceraldehyde-3-P...

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Spencer PW, Spencer RD. Globulin-specific Proteolytic Activity in Germinating Pumpkin Seeds as Detected by a Fluorescence Assay Method. Plant Physiol. 1974;54(6):925-30doi: 10.1104/pp.54.6.925.
Spencer, P. W., & Spencer, R. D. (1974). Globulin-specific Proteolytic Activity in Germinating Pumpkin Seeds as Detected by a Fluorescence Assay Method. Plant physiology, 54(6), 925-30. https://doi.org/10.1104/pp.54.6.925
Spencer, P W, and Spencer, R D. "Globulin-specific Proteolytic Activity in Germinating Pumpkin Seeds as Detected by a Fluorescence Assay Method." Plant physiology vol. 54,6 (1974): 925-30. doi: https://doi.org/10.1104/pp.54.6.925
Spencer PW, Spencer RD. Globulin-specific Proteolytic Activity in Germinating Pumpkin Seeds as Detected by a Fluorescence Assay Method. Plant Physiol. 1974 Dec;54(6):925-30. doi: 10.1104/pp.54.6.925. PMID: 16659002; PMCID: PMC366635.
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Ion association reactions with biological membranes, studied with the fluorescent dye 1-anilino-8-naphthalenesulfonate.

The Journal of membrane biology

Gomperts B, Lantelme F, Stock R.
PMID: 24174196
J Membr Biol. 1970 Dec;3(1):241-66. doi: 10.1007/BF01868018.

(1) When salts are added to buffered suspensions of membrane fragments containing the fluorochrome 1-anilino-8-naphthalenesulfonate (ANS), there is an increased fluorescence. This is caused by increased binding of the fluorochrome; the intrinsic fluorescence characteristics of the bound dye remain...

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Gomperts B, Lantelme F, Stock R. Ion association reactions with biological membranes, studied with the fluorescent dye 1-anilino-8-naphthalenesulfonate. J Membr Biol. 1970;3(1):241-66doi: 10.1007/BF01868018.
Gomperts, B., Lantelme, F., & Stock, R. (1970). Ion association reactions with biological membranes, studied with the fluorescent dye 1-anilino-8-naphthalenesulfonate. The Journal of membrane biology, 3(1), 241-66. https://doi.org/10.1007/BF01868018
Gomperts, B, et al. "Ion association reactions with biological membranes, studied with the fluorescent dye 1-anilino-8-naphthalenesulfonate." The Journal of membrane biology vol. 3,1 (1970): 241-66. doi: https://doi.org/10.1007/BF01868018
Gomperts B, Lantelme F, Stock R. Ion association reactions with biological membranes, studied with the fluorescent dye 1-anilino-8-naphthalenesulfonate. J Membr Biol. 1970 Dec;3(1):241-66. doi: 10.1007/BF01868018. PMID: 24174196.
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Interaction of cyclotide Kalata B1 protein with model cellular membranes of varied electrostatics.

International journal of biological macromolecules

Gupta R, Kumari J, Pati S, Singh S, Mishra M, Ghosh SK.
PMID: 34592223
Int J Biol Macromol. 2021 Nov 30;191:852-860. doi: 10.1016/j.ijbiomac.2021.09.147. Epub 2021 Sep 27.

A uni-molecular layer of lipids at air-water interface mimicking one of the leaflets of the cellular membrane provides a simple model to understand the interaction of any foreign molecules with the membrane. Here, the interactions of protein Kalata B1...

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Gupta R, Kumari J, Pati S, et al. Interaction of cyclotide Kalata B1 protein with model cellular membranes of varied electrostatics. Int J Biol Macromol. 2021;191:852-860doi: 10.1016/j.ijbiomac.2021.09.147.
Gupta, R., Kumari, J., Pati, S., Singh, S., Mishra, M., & Ghosh, S. K. (2021). Interaction of cyclotide Kalata B1 protein with model cellular membranes of varied electrostatics. International journal of biological macromolecules, 191852-860. https://doi.org/10.1016/j.ijbiomac.2021.09.147
Gupta, Ritika, et al. "Interaction of cyclotide Kalata B1 protein with model cellular membranes of varied electrostatics." International journal of biological macromolecules vol. 191 (2021): 852-860. doi: https://doi.org/10.1016/j.ijbiomac.2021.09.147
Gupta R, Kumari J, Pati S, Singh S, Mishra M, Ghosh SK. Interaction of cyclotide Kalata B1 protein with model cellular membranes of varied electrostatics. Int J Biol Macromol. 2021 Nov 30;191:852-860. doi: 10.1016/j.ijbiomac.2021.09.147. Epub 2021 Sep 27. PMID: 34592223.
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Synthesis of a Three-Helix Bundle Protein by Reductive Amination.

The Journal of organic chemistry

Tahmassebi DC, Sasaki T.
PMID: 11672067
J Org Chem. 1998 Feb 06;63(3):728-731. doi: 10.1021/jo970812m.

An organic trialdehyde, TRIPOD (2), was designed as a template for the synthesis of a three-helix bundle protein. Crystallographic data indicate that the aldehyde groups are appropriately spaced to maximize hydrophobic interactions between the chains of the protein. Peptide...

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Tahmassebi DC, Sasaki T. Synthesis of a Three-Helix Bundle Protein by Reductive Amination. J Org Chem. 1998;63(3):728-731doi: 10.1021/jo970812m.
Tahmassebi, D. C., & Sasaki, T. (1998). Synthesis of a Three-Helix Bundle Protein by Reductive Amination. The Journal of organic chemistry, 63(3), 728-731. https://doi.org/10.1021/jo970812m
Tahmassebi, Deborah C., and Sasaki, Tomikazu. "Synthesis of a Three-Helix Bundle Protein by Reductive Amination." The Journal of organic chemistry vol. 63,3 (1998): 728-731. doi: https://doi.org/10.1021/jo970812m
Tahmassebi DC, Sasaki T. Synthesis of a Three-Helix Bundle Protein by Reductive Amination. J Org Chem. 1998 Feb 06;63(3):728-731. doi: 10.1021/jo970812m. PMID: 11672067.
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The interaction of 1-anilino-8-naphthalenesulfonate with the membranes of the sarcoplasmic reticulum and various lipid compounds.

The Journal of membrane biology

Hasselbach W, Heimberg KW.
PMID: 24174156
J Membr Biol. 1970 Dec;2(1):341-50. doi: 10.1007/BF01869869.

(1) The enzymatic removal of lipids from the vesicular membranes of the sarcoplasmic reticulum does not interfere with the fluorescence of the 1-anilino-8-naphthalenesulfonate (ANS) vesicular complex. (2) The fluorescence intensity of the ANS vesicular complex is considerably (50%) reduced...

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Hasselbach W, Heimberg KW. The interaction of 1-anilino-8-naphthalenesulfonate with the membranes of the sarcoplasmic reticulum and various lipid compounds. J Membr Biol. 1970;2(1):341-50doi: 10.1007/BF01869869.
Hasselbach, W., & Heimberg, K. W. (1970). The interaction of 1-anilino-8-naphthalenesulfonate with the membranes of the sarcoplasmic reticulum and various lipid compounds. The Journal of membrane biology, 2(1), 341-50. https://doi.org/10.1007/BF01869869
Hasselbach, W, and Heimberg, K W. "The interaction of 1-anilino-8-naphthalenesulfonate with the membranes of the sarcoplasmic reticulum and various lipid compounds." The Journal of membrane biology vol. 2,1 (1970): 341-50. doi: https://doi.org/10.1007/BF01869869
Hasselbach W, Heimberg KW. The interaction of 1-anilino-8-naphthalenesulfonate with the membranes of the sarcoplasmic reticulum and various lipid compounds. J Membr Biol. 1970 Dec;2(1):341-50. doi: 10.1007/BF01869869. PMID: 24174156.
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Temperature-jump investigation of alkyl chain length effects on sorption/desorption kinetics at reversed-phase chromatographic interfaces.

Analytical chemistry

Ren FY, Harris JM.
PMID: 21619132
Anal Chem. 1996 May 01;68(9):1651-7. doi: 10.1021/ac950935b.

The influence of the alkyl chain length on the kinetics of solute retention at reversed-phase chromatographic surfaces is examined. A Joule-discharge temperature-jump relaxation experiment was used to monitor reversible sorption/desorption kinetics at C4- and C8-modified silica/solution interfaces. Biexponential sorption/desorption...

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Ren FY, Harris JM. Temperature-jump investigation of alkyl chain length effects on sorption/desorption kinetics at reversed-phase chromatographic interfaces. Anal Chem. 1996;68(9):1651-7doi: 10.1021/ac950935b.
Ren, F. Y., & Harris, J. M. (1996). Temperature-jump investigation of alkyl chain length effects on sorption/desorption kinetics at reversed-phase chromatographic interfaces. Analytical chemistry, 68(9), 1651-7. https://doi.org/10.1021/ac950935b
Ren, F Y, and Harris, J M. "Temperature-jump investigation of alkyl chain length effects on sorption/desorption kinetics at reversed-phase chromatographic interfaces." Analytical chemistry vol. 68,9 (1996): 1651-7. doi: https://doi.org/10.1021/ac950935b
Ren FY, Harris JM. Temperature-jump investigation of alkyl chain length effects on sorption/desorption kinetics at reversed-phase chromatographic interfaces. Anal Chem. 1996 May 01;68(9):1651-7. doi: 10.1021/ac950935b. PMID: 21619132.
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Two distinguishable fluorescent modes of 1-anilino-8-naphthalenesulfonate bound to human albumin.

Journal of fluorescence

Bagatolli LA, Kivatinitz SC, Aguilar F, Soto MA, Sotomayor P, Fidelio GD.
PMID: 24226995
J Fluoresc. 1996 Mar;6(1):33-40. doi: 10.1007/BF00726724.

We study the interaction of 1-anilino-8-naphthalenesulfonate (ANS) with human (HSA) and bovine serum albumin (BSA) by phase and modulation fluorescence spectroscopy. We determined that both HSA and BSA show one or two distinguishable fluorescent sites, depending of the ANS/serum...

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Bagatolli LA, Kivatinitz SC, Aguilar F, et al. Two distinguishable fluorescent modes of 1-anilino-8-naphthalenesulfonate bound to human albumin. J Fluoresc. 1996;6(1):33-40doi: 10.1007/BF00726724.
Bagatolli, L. A., Kivatinitz, S. C., Aguilar, F., Soto, M. A., Sotomayor, P., & Fidelio, G. D. (1996). Two distinguishable fluorescent modes of 1-anilino-8-naphthalenesulfonate bound to human albumin. Journal of fluorescence, 6(1), 33-40. https://doi.org/10.1007/BF00726724
Bagatolli, L A, et al. "Two distinguishable fluorescent modes of 1-anilino-8-naphthalenesulfonate bound to human albumin." Journal of fluorescence vol. 6,1 (1996): 33-40. doi: https://doi.org/10.1007/BF00726724
Bagatolli LA, Kivatinitz SC, Aguilar F, Soto MA, Sotomayor P, Fidelio GD. Two distinguishable fluorescent modes of 1-anilino-8-naphthalenesulfonate bound to human albumin. J Fluoresc. 1996 Mar;6(1):33-40. doi: 10.1007/BF00726724. PMID: 24226995.
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Showing 1 to 7 of 7 entries