Specific Group Reagents for Proteins.

Olcott, Henry Steel; Fraenkel‐Conrat, H.

doi:10.1021/cr60128a004

Cited by 223 publications

(67 citation statements)

References 127 publications

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“…However, some preparations with a low concentration of enzyme were more active with lactic acid. The data are summarized in (1,7). In all tests, these inhibitors were added to a buffered enzyme preparation (either the barley juice or the purified spinach enzyme previously reconstituted by the addition of riboflavin monophosphate) and incubated for 30 minutes at 30°C before addition of substrate.…”

Section: Experimental Results Survey Of Plants For Glycolic Acid Oxidmentioning

confidence: 99%

Nature and Distribution of Glycolic Acid Oxidase in Plants.

Noll

Burris

1954

Plant Physiol.

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Section: Experimental Results Survey Of Plants For Glycolic Acid Oxidmentioning

confidence: 99%

Nature and Distribution of Glycolic Acid Oxidase in Plants.

Noll

Burris

1954

Plant Physiol.

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“…In general, if the primary structure of protein is still intact it may be possible to recover its original three-dimensional conformation under an optimal retrieval system. Because crosslinkages are complicated processes that depend on a variety of conditions (e.g., pH, temperature, conditions of tissue and fixation), they may lead to a variety of protein alterations ,1948aOlcott and Fraenkel-Conrat 1947). Therefore, the use of a test battery is recommended to solve this complicated situation.…”

Section: Study Of the Mechanism Of Armentioning

confidence: 99%

Antigen Retrieval Immunohistochemistry: Past, Present, and Future

Shi

Côté²,

Taylor

1997

J Histochem Cytochem.

480

331

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SUMMARYThe antigen retrieval (AR) technique, which is predominantly based on hightemperature heating of tissues, is used as a non-enzymatic pretreatment for immunohistochemical staining of formalin-fixed, paraffin-embedded tissue sections. It has been widely applied in pathology and analytical morphology. The existence of a growing body of literature on the AR technique raises a number of interesting issues for the further development of AR. These issues include the use of a "test battery" and the concept of "maximal retrieval" applied to the selection of optimal test protocols for the standardization of AR. (J Histochem Cytochem 45:327-343, 1997)

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“…The use of TNBS1 for the determination of amino groups (47) and DTNB for the determination of thiol groups (48) Those interests and further careful scrutiny of the available methodology led to the publication of two important reviews of protein modification in 1947 (49,50). The report of Balls and Jansen (51) showing that the inactivation of several proteases by diisopropyl fluorophosphate resulted from its reaction with a specific serine residue in each case was another milestone of this period.…”

Section: Early Developmentsmentioning

confidence: 99%

Chemical modifications of proteins: history and applications

Means¹,

Feeney²

1990

Bioconjugate Chem.

181

170

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With roots in ancient formulations, methods for the chemical derivatization of proteins continue to expand and develop. The creation of this new journal dealing exclusively with bioconjugate chemistry was barely conceivable just a few years ago. An explosion of interest in the subject during the last decade is, however, easily seen. The tremendous growth in both the number of publications and in the number of research groups involved in these kinds of studies has been promoted by both practical interests related, for example, in some cases to possible pharmacological or medical diagnostic applications and by interest in questions of fundamental biochemical structure and function.Greatly Reagents have been designed to preserve electrostatic charge (4,5), to alter electrostatic charge (6), and to increase hydrophobicity (7,8). Reagents and procedures have been developed to decrease immunogenicity (9, 20), to increase and decrease susceptibility to proteolysis (22-23), to increase UV or visible absorbancy (14), to introduce fluorescent labels (25,16), spin labels (27), radiolabels , various metal ions (22), magnetic microspheres (22,23), and electron-dense substituents (24), to increase the content of certain low-abundance nonradioactive isotopes (25)

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Specific Group Reagents for Proteins.

Cited by 223 publications

References 127 publications

Nature and Distribution of Glycolic Acid Oxidase in Plants.

Nature and Distribution of Glycolic Acid Oxidase in Plants.

Antigen Retrieval Immunohistochemistry: Past, Present, and Future

Chemical modifications of proteins: history and applications

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