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We have obtained a crude enzyme preparation from bovine parathyroid gland homogenates which when incubated with PTH, cleaves the hormone into two major fragments. Isolation and chemical analysis has led to the identification of these peptides, the 1-34 fragment and the 35-84 fragment. Digestion of PTH was totally inhibited by the inclusion of the cathepsin D inhibitor, pepstatin, in the enzyme digest. A comparison of the digest obtained using the crude enzyme fraction vs. digestion of PTH by purified bovine cathepsin D led to the findings that the same peptide products were formed in each case. The natural 1-34 hormone fragment derived from the procedure has been determined to be fully biologically active in a bone resorption system.
J W Hamilton, and
R L Jilka, and
R R MacGregor
August 1983,
The Journal of biological chemistry,
J W Hamilton, and
R L Jilka, and
R R MacGregor
February 1985,
The Journal of biological chemistry,
J W Hamilton, and
R L Jilka, and
R R MacGregor
May 2003,
The Journal of clinical endocrinology and metabolism,
J W Hamilton, and
R L Jilka, and
R R MacGregor
July 1982,
The Journal of endocrinology,
J W Hamilton, and
R L Jilka, and
R R MacGregor
March 1985,
General and comparative endocrinology,
J W Hamilton, and
R L Jilka, and
R R MacGregor
July 1980,
Endocrinology,
J W Hamilton, and
R L Jilka, and
R R MacGregor
January 2000,
Biochemical and biophysical research communications,
J W Hamilton, and
R L Jilka, and
R R MacGregor
January 1976,
Endocrine research communications,
J W Hamilton, and
R L Jilka, and
R R MacGregor
December 1991,
The Journal of clinical endocrinology and metabolism,
J W Hamilton, and
R L Jilka, and
R R MacGregor
April 1991,
Calcified tissue international,
