Spin-labeling of porcine pepsin and rhizopus chinensis acid protease by diazoketone reagents

Nakayama, Shinichi; Nagashima, Youko; Hoshino, Minoru; Moriyama, Akihiko; Takahashi, Kenji; Uematsu, Yasuko; Watanabe, Tokuko; Yoshida, Masayuki

doi:10.1016/0006-291x(81)91309-7

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Aspartic Proteinases1

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1982

1994

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Cited by 3 publications

(1 citation statement)

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“…With some, labeled inhibitors have been used to isolate active-site peptides and to directly demonstrate the involvement of one or two aspartic acid residues (152,185,224). Recently, diazoketone reagents have been used for active-site spin labeling of the proteinase from Rhizopus chinensis (226). Not every acid proteinase is inhibited by the specific inhibitors pepstatin or Streptomyces pepsin inhibitor (S-PI), and a small but significant group of insensitive enzymes has now been reported: proteinase A of Aspergillus niger var.…”

Section: Aspartic Proteinasesmentioning

confidence: 99%

Comparative biochemistry of the proteinases of eucaryotic microorganisms.

North¹

1982

Microbiological Reviews

196

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Section: Aspartic Proteinasesmentioning

confidence: 99%

Comparative biochemistry of the proteinases of eucaryotic microorganisms.

North¹

1982

Microbiological Reviews

196

View full text Add to dashboard Cite

Arginyl residues are involved in the transport of Fe2+ through the plasma membrane of the mammalian reticulocyte

González-Sepúlveda

Núñez

1994

J. Membarin Biol.

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Sealed reticulocyte ghosts were treated with reagents that modify a variety of amino acid residues. Only ninhydrin and phenylglyoxal, both modifiers of arginyl residues, produced inhibition of the initial rate of 59Fe2+ uptake. The inhibition (i) was dependent on the concentration of ninhydrin or phenylglyoxal, (ii) increased from pH 7 to 9, a feature of the modification of arginine by ninhydrin or phenylglyoxal, and (iii) was blocked when Fe2+ was present during the modification step. A23187, an effective membrane Fe2+ transporter, diminished the inhibitory effect of ninhydrin and phenylglyoxal, indicative that the transport of iron through the membrane, and not a secondary process, was selectively inhibited. We conclude that the iron transporter from the plasma membrane of erythroid cells has one or more arginyl residues in a segment accessible to ninhydrin or phenylglyoxal, and that this residue is involved in the transmembrane transport of iron.

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Comparative biochemistry of the proteinases of eucaryotic microorganisms

North¹

1982

Microbiol Rev

165

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Spin-labeling of porcine pepsin and rhizopus chinensis acid protease by diazoketone reagents

Cited by 3 publications

References 14 publications

Comparative biochemistry of the proteinases of eucaryotic microorganisms.

Comparative biochemistry of the proteinases of eucaryotic microorganisms.

Arginyl residues are involved in the transport of Fe2+ through the plasma membrane of the mammalian reticulocyte

Comparative biochemistry of the proteinases of eucaryotic microorganisms

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