A nonfunctional protein in human leukemia cells reacts with antiserum to dihydrofolate reductase from L1210 leukemia cells

M. Perwaiz Iqbal; Sheldon P. Rothenberg

doi:10.1016/0024-3205(81)90021-7

A nonfunctional protein in human leukemia cells reacts with antiserum to dihydrofolate reductase from L1210 leukemia cells

M. Perwaiz Iqbal, Sheldon P. Rothenberg

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

Abstract

Antiserum raised in chickens to dihydrofolate reductase purified from L1210 leukemia cells by affinity chromatography inhibited the catalytic activity and the binding of methotrexate by the enzyme. Lysates of human chronic myelogenous leukemia cells, which had neither catalytic activity for dihydrofolate reductase nor binding of methotrexate, blocked the inhibiting effect of the antiserum on the function of the enzyme in L1210 cell lysates. In double immunodiffusion, these human leukemia cell lysates formed a single precipitin line against the antiserum. These findings indicate that nonfunctional dihydrofolate reductase in human leukemia cells share an antigenic determinant(s) with a functional form of the enzyme from L1210 murine leukemia cells.

Original language	English
Pages (from-to)	689-696
Number of pages	8
Journal	Life Sciences
Volume	29
Issue number	7
DOIs	https://doi.org/10.1016/0024-3205(81)90021-7
Publication status	Published - 17 Aug 1981
Externally published	Yes

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title = "A nonfunctional protein in human leukemia cells reacts with antiserum to dihydrofolate reductase from L1210 leukemia cells",

abstract = "Antiserum raised in chickens to dihydrofolate reductase purified from L1210 leukemia cells by affinity chromatography inhibited the catalytic activity and the binding of methotrexate by the enzyme. Lysates of human chronic myelogenous leukemia cells, which had neither catalytic activity for dihydrofolate reductase nor binding of methotrexate, blocked the inhibiting effect of the antiserum on the function of the enzyme in L1210 cell lysates. In double immunodiffusion, these human leukemia cell lysates formed a single precipitin line against the antiserum. These findings indicate that nonfunctional dihydrofolate reductase in human leukemia cells share an antigenic determinant(s) with a functional form of the enzyme from L1210 murine leukemia cells.",

author = "{Perwaiz Iqbal}, M. and Rothenberg, {Sheldon P.}",

note = "Funding Information: This work was supported by Grant CA 08976, awarded by the National Cancer Institute, DHEW. Mr. Iqbal submitted this research to satisfy the requirements toward his Master's Degree at New York University under Dr. Vinay Likhite, Faculty Advisor.",

year = "1981",

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doi = "10.1016/0024-3205(81)90021-7",

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T1 - A nonfunctional protein in human leukemia cells reacts with antiserum to dihydrofolate reductase from L1210 leukemia cells

AU - Perwaiz Iqbal, M.

AU - Rothenberg, Sheldon P.

N1 - Funding Information: This work was supported by Grant CA 08976, awarded by the National Cancer Institute, DHEW. Mr. Iqbal submitted this research to satisfy the requirements toward his Master's Degree at New York University under Dr. Vinay Likhite, Faculty Advisor.

PY - 1981/8/17

Y1 - 1981/8/17

N2 - Antiserum raised in chickens to dihydrofolate reductase purified from L1210 leukemia cells by affinity chromatography inhibited the catalytic activity and the binding of methotrexate by the enzyme. Lysates of human chronic myelogenous leukemia cells, which had neither catalytic activity for dihydrofolate reductase nor binding of methotrexate, blocked the inhibiting effect of the antiserum on the function of the enzyme in L1210 cell lysates. In double immunodiffusion, these human leukemia cell lysates formed a single precipitin line against the antiserum. These findings indicate that nonfunctional dihydrofolate reductase in human leukemia cells share an antigenic determinant(s) with a functional form of the enzyme from L1210 murine leukemia cells.

AB - Antiserum raised in chickens to dihydrofolate reductase purified from L1210 leukemia cells by affinity chromatography inhibited the catalytic activity and the binding of methotrexate by the enzyme. Lysates of human chronic myelogenous leukemia cells, which had neither catalytic activity for dihydrofolate reductase nor binding of methotrexate, blocked the inhibiting effect of the antiserum on the function of the enzyme in L1210 cell lysates. In double immunodiffusion, these human leukemia cell lysates formed a single precipitin line against the antiserum. These findings indicate that nonfunctional dihydrofolate reductase in human leukemia cells share an antigenic determinant(s) with a functional form of the enzyme from L1210 murine leukemia cells.

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DO - 10.1016/0024-3205(81)90021-7

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A nonfunctional protein in human leukemia cells reacts with antiserum to dihydrofolate reductase from L1210 leukemia cells

Abstract

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