Analytic Immunologic Techniques

Kunkel, Joseph G.

doi:10.1007/978-1-4612-3798-3_1

Cited by 4 publications

(7 citation statements)

References 92 publications

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“…The NH2-terminal amino acid sequences of the purified P-450s were identical to each other in the first 19 positions from their amino terminal ends: MLLLLLLIVVTTLYIFAKL ( Table 2). This agrees with the sequence previously reported for P-4501p, [26].…”

Section: Nhtterminal Sequencementioning

confidence: 98%

“…The P-450s purified here had a high hydrophobic nature in the NH2-terminal region. Specifically, 15 (79%) of the 19 amino acid residues in the N-terminus were hydrophobic amino acids. Interestingly, 42% of the amino acids in this region were leucine.…”

Section: Nhtterminal Sequencementioning

confidence: 99%

“…Normal rabbit antiserum which had been partially purified twice wth ammonium sulfate precipitation [19] was used to adjust the volume of total antisera to 32 pl in the incubates and 68 p1 of 0.1 M sodium phosphate buffer (pH 7.5) was added. Seventy-one microliters ( = 50 pmol of total cytochrome P-450 content) of this incubate were then aliquoted and used for assay of ECOD activity as described earlier.…”

Section: Trnmunoinhibition Studiesmentioning

confidence: 99%

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Purification and characterization of a cytochrome P‐450 from insecticide susceptible and resistant strains of housefly, Musca domestica L., before and after phenobarbital exposure

Scott

Lee

1993

Arch Insect Biochem Physiol

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A cytochrome P-450 (P-450) was purified from abdominal microsomes of untreated and phenobarbital treated susceptible (S+) and insecticide-resistant (LPR) houseflies using HPLC purification procedures. The purified P-450s exhibited the same apparent molecular masses (54,400 dalton) and could not be distinguished from each other on the basis of HPLC chromatographic properties, reduced CO-difference absorbance maxima (447 +/- 0.5 nm), or partial NH2-terminal sequences (MLLLLLLIVVTTLYIFAKL). Since these P-450s were indistinguishable and were immunologically identical to cytochrome P-450lpr we conclude that these P-450s are in fact cytochrome P-450lpr. The level of P-450lpr was increased twofold after PB exposure in the S+ strain, while the level of P-450lpr did not change in the LPR strain. Immunoinhibition of ECOD activity with anti-P-450lpr antiserum suggests that PB treatment in S+ house flies induced P-450lpr, and other forms of cytochromes P-450 with high activity toward this substrate.

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Section: Nhtterminal Sequencementioning

confidence: 98%

Section: Nhtterminal Sequencementioning

confidence: 99%

Section: Trnmunoinhibition Studiesmentioning

confidence: 99%

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Purification and characterization of a cytochrome P‐450 from insecticide susceptible and resistant strains of housefly, Musca domestica L., before and after phenobarbital exposure

Scott

Lee

1993

Arch Insect Biochem Physiol

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“…Specific antisera against Lymun tria dispar Ap were made against purified L. dispav Ap [7,8]. Specific antisera against Manducu sexta Ap and M .…”

Section: Immunblogical Techniquementioning

confidence: 99%

“…Some minor [6] or major [7] cycling of Ap has been observed in association with each larval molting cycle in certain Lepidoptera. This protein has been ascribed a role of providing one of the physical resources of amino acids for reorganization during the nonfeeding pupal stage [8,9]. High Ap is diagnostic of the onset of metamorphosis in all Lepidoptera studied to date.…”

Section: Introductionmentioning

confidence: 98%

Arylphorin of Trichoplusia ni: Characterization and parasite‐induced precocious increase in titer

Kunkel

Grossniklaus-Buergin

Karpells

et al. 1990

Arch Insect Biochem Physiol

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Anti‐P450_lpr antiserum inhibits specific monooxygenase activities in LPR house fly microsomes

Wheelock

Scott

1992

J. Exp. Zool.

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Monooxygenase activity in microsomes from the LPR strain of house fly (Musca domestica L.) was inhibited by anti-P450lpr, and antiserum specific for house fly cytochrome P450lpr. Anti-P450lpr did not inhibit house fly cytochrome P450 reductase or rat cytochrome P450 monooxygenase assays, consistent with specific inhibition of P450lpr. Anti-P450lpr inhibited the ability of cytochrome P450 reductase to reduce carbon monoxide treated LPR microsomal cytochrome P450, up to 49% of the total, showing that inhibition of cytochrome P450 reduction is the major mechanism of inhibition. Anti-P450lpr inhibited 98% of methoxyresorufin-O-demethylase activity and all the benzo(a)pyrene hydroxylase activity in LPR microsomes, but none of the pentoxyresorufin-O-dealkylase activity. The antiserum partially inhibited ethoxyresorufin-O-dealkylase and ethoxycoumarin-O-dealkylase activity. These results demonstrate that methoxyresourfin-O-demethylase activity and benzo(a)pyrene hydroxylase activity are characteristic substrates for P450lpr activity in the LPR strain of house fly.

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Analytic Immunologic Techniques

Cited by 4 publications

References 92 publications

Purification and characterization of a cytochrome P‐450 from insecticide susceptible and resistant strains of housefly, Musca domestica L., before and after phenobarbital exposure

Purification and characterization of a cytochrome P‐450 from insecticide susceptible and resistant strains of housefly, Musca domestica L., before and after phenobarbital exposure

Arylphorin of Trichoplusia ni: Characterization and parasite‐induced precocious increase in titer

Anti‐P450_lpr antiserum inhibits specific monooxygenase activities in LPR house fly microsomes

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Analytic Immunologic Techniques

Cited by 4 publications

References 92 publications

Purification and characterization of a cytochrome P‐450 from insecticide susceptible and resistant strains of housefly, Musca domestica L., before and after phenobarbital exposure

Purification and characterization of a cytochrome P‐450 from insecticide susceptible and resistant strains of housefly, Musca domestica L., before and after phenobarbital exposure

Arylphorin of Trichoplusia ni: Characterization and parasite‐induced precocious increase in titer

Anti‐P450lpr antiserum inhibits specific monooxygenase activities in LPR house fly microsomes

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Anti‐P450_lpr antiserum inhibits specific monooxygenase activities in LPR house fly microsomes