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Blood, 1974, Vol. 44, No. 2, pp. 235-246.
© 1974 American Society of Hematology, Inc.
Cationic Proteins of Human Granulocytes.
II. Separation of the Cationic Proteins of the
Granules of Leukemic Myeloid Cells
I. Olsson 1 and
P. Venge 1
1 Department of Internal Medicine and Research Laboratory for Clinical Hematology,
University of Lund, and Department of Clinical Chemistry, University of Uppsala, Sweden.
The highly cationic proteins of human
granulocytes, whose electrophoretic mobilities toward the cathode are faster than
that for lysozyme, were isolated from the
cytoplasmic granules of leukocytes, obtained from patients with chronic myeloid
leukemia. The granule extract was subjected to chromatography on Sephadex
G-75 and E-aminocaproic acid-Sepharose
ion adsorbant followed by preparative
electrophoresis on agarose. Seven cationic
protein components were identified, and
five of these were obtained in a pure form.
One group of cationic proteins, including
components 1-4, exhibited molecular
weights in the range 25,500-28,500,
almost identical amino acid composition,
and complete immunologic identity.
Another group of proteins, including components 5-7, exhibited molecular weights
in the range 21,000-29,000 and also
showed complete immunologic identity;
amino acid analysis performed on component 5 indicated a different amino acid
composition from that of components 1-4.
Cationic proteins with similar electrophoretic mobilities and immunochemical
identities were also detected in granule
extracts of granulocytes from healthy
individuals. The proteins isolated from
human granulocytes have a higher molecular weight and a lower content of
basic amino acids than the cationic proteins with antibacterial and permeability-increasing properties previously demonstrated in rabbit polymorphonuclear
granulocytes.
Submitted on June 18, 1973
Revised on December 10, 1973
Accepted on February 21, 1974
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