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Human splenic galaptin: physicochemical characterization.

A Sharma1, R Chemelli, H J Allen

  • 1Department of Surgical Oncology, Roswell Park Memorial Institute, Buffalo, New York 14263.

Biochemistry
|June 5, 1990
PubMed
Summary
This summary is machine-generated.

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Human splenic galaptin, a beta-galactoside-binding lectin, was found to be identical to human placental galaptin. This 14.5 kDa lectin is also present in other mammalian spleens.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Beta-galactoside-binding lectins are present in mammalian spleens.
  • Human splenic galaptin's relationship to other lectins was previously undetermined.

Purpose of the Study:

  • To determine the relationship of human splenic galaptin to other beta-galactoside-binding lectins.
  • To characterize human splenic galaptin.

Main Methods:

  • SDS-PAGE, RP-HPLC, and Western blot analyses were used to identify and characterize galaptin in human spleen.
  • Isoelectric focusing, UV spectral analysis, circular dichroic analysis, and amino acid sequencing were performed on purified galaptin.
  • Western blot analysis with anti-human splenic galaptin antiserum was used to detect related polypeptides in other mammalian spleens.

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Main Results:

  • Human spleen contained a single beta-galactoside-binding lectin of 14.5 kDa, identified as galaptin.
  • Purified galaptin showed three polypeptides with pI values of 4.60, 4.80, and 4.85 (major band at 4.85).
  • Amino acid sequence analysis revealed that human splenic galaptin is identical to human placental galaptin. A related 14.5 kDa polypeptide was detected in other mammalian spleens.

Conclusions:

  • Human splenic galaptin is identical to human placental galaptin.
  • A related lectin is present in the spleens of various mammals.