Reductive alkylation of proteins

Means, Gary E.

doi:10.1007/bf01024842

Cited by 33 publications

(22 citation statements)

References 57 publications

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“…This reduction is generally accomplished using NaBH 4 or NaCNBH 3 , which react optimally at basic or neutral pH values, respectively. [92] Oximes and hydrazones are hydrolytically stable between pH 2-7 and 5-7, respectively, but they decompose rapidly above pH 9. [93,94] Aldehyde-functionalized polymers can be conveniently prepared from 3,3'-diethoxypropyl methacrylate, which can be polymerized using freeradical polymerization [95] as well as under ATRP [96] and RAFT [97] conditions.…”

Section: Modification Of Polymers Bearing Aldehydes and Ketonesmentioning

confidence: 99%

Synthesis of Functional Polymers by Post‐Polymerization Modification

2008

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Post-polymerization modification is based on the direct polymerization or copolymerization of monomers bearing chemoselective handles that are inert towards the polymerization conditions but can be quantitatively converted in a subsequent step into a broad range of other functional groups. The success of this method is based on the excellent conversions achievable under mild conditions, the excellent functional-group tolerance, and the orthogonality of the post-polymerization modification reactions. This Review surveys different classes of reactive polymer precursors bearing chemoselective handles and discusses issues related to the preparation of these reactive polymers by direct polymerization of appropriately functionalized monomers as well as the post-polymerization modification of these precursors into functional polymers.

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Section: Modification Of Polymers Bearing Aldehydes and Ketonesmentioning

confidence: 99%

Synthesis of Functional Polymers by Post‐Polymerization Modification

2008

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“…These considerations have led to the development of numerous new delivery technologies, including particulate controlled release systems such as liposomes [Alving et al, 1992], emulsions, and MS [Tomiya et al, 1985] and chemical modification of proteins [Mean and Feeney, 1995]. Polymeric MS is a promising delivery system for the protection and release of proteins [Cohen et al, 1991].…”

Section: As a Model Polymer Proteinmentioning

confidence: 99%

Biopolymer albumin for diagnosis and in drug delivery

Patil¹

2003

Drug Development Research

156

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This article reviews the developmental stages and strategies used to assess the biomedical utility of biopolymer albumin from the 1970s to early 2002. The basic method and mechanism(s) of preparation of albumin microspheres and subsequent modifications made to overcome the drawbacks of earlier approaches and the need for further developments are discussed, as are the processing parameters and the level of various ingredients affecting the physicochemical properties of the albumin microspheres. Different equations proposed by various investigators to modulate in vitro release kinetics are reviewed. The microscopic structural and surface properties, the chemical modification of the biopolymer (e.g., cationization, tagging with amino acids and sugar moieties) for tissue specificity or to influence the release profile and biodegradation are discussed. An array of potential diagnostic applications and the use of albumin microspheres as a drug delivery system are reviewed. Drug Dev.

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“…This was carried out essentially as described by Means and Feeney (1968). To 1 mL of purified S1 nuclease (200 pg) in 200 mM sodium borate buffer (pH 9.0) at O"C, 0.1 ml of sodium borohydride (0.5 mg/mL) was added followed by the addition of six aliquots (20 pL each) of 0.35% (v/v) formaldehyde solution, at an interval of 10 rnin.…”

Section: Affinity Labeling Studiesmentioning

confidence: 99%

S1 nuclease: Immunoaffinity purification and evidence for the proximity of cysteine 25 to the substrate binding site

Gite

Shankar

1995

J of Molecular Recognition

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A simple procedure, involving heat treatment, gel filtration on Sephadex-G 100 followed by chromatography on anti-S1 nuclease antibodies bound to Sepharose, was developed for purification of S1 nuclease to homogeneity with an overall yield of 72%. S1 nuclease was rapidly inactivated, at pH 6.0 and 37 degrees C, in presence of o-phthalaldehyde. Kinetic analysis of o-phthalaldehyde medicated inactivation showed that the reaction followed pseudo-first-order kinetics and the loss of enzyme activity was due to the formation of a single isoindole derivative per molecule of the enzyme. Absorbance and fluorescence spectrophotometric data also gave similar results. The isoindole derivative formation, as a result of o-phthalaldehyde treatment is known to occur through crosslinking of the thiol group of cysteine and the epsilon-amino group of lysine, situated in close proximity in the native enzyme. Since, modification of the only available cysteine residue (Cys25) did not affect the catalytic activity of the enzyme, the o-phthalaldehyde mediated inactivation of S1 nuclease is due to the modification of lysine. Substrates of S1 nuclease, namely ssDNA, RNA, 3'AMP, could protect the enzyme against o-phthalaldehyde mediated inactivation. Moreover, the modified enzyme (having very little catalytic activity) showed a significant decrease in its ability to bind 5'AMP, a competitive inhibitor of S1 nuclease, suggesting that the modification has occurred at the substrate binding site. The above results point towards the presence of cysteine 25 in close proximity to the substrate binding site.

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Reductive alkylation of proteins

Cited by 33 publications

References 57 publications

Synthesis of Functional Polymers by Post‐Polymerization Modification

Synthesis of Functional Polymers by Post‐Polymerization Modification

Biopolymer albumin for diagnosis and in drug delivery

S1 nuclease: Immunoaffinity purification and evidence for the proximity of cysteine 25 to the substrate binding site

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