Crystallization of cathepsin D

Kazakova, O. V.; Orokhovich, V.N.

doi:10.1016/s0006-291x(76)80102-7

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B Other Acid Proteinases1

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1979

1984

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Cited by 18 publications

(1 citation statement)

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“…This enzyme has been purified, and several isozymes have been identified (282)(283)(284); its crystallization has also been reported (285). A limited number of synthetic peptides have been tested as substrates of cathepsin D, and the available data indicate that its primary and secondary specificities resemble that of pepsin (282,286).…”

Section: B Other Acid Proteinasesmentioning

confidence: 99%

Proteinase‐Catalyzed Synthesis of Peptide Bonds

Fruton

1982

Advances in Enzymology - And Related Areas of Molecular Biology

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Section: B Other Acid Proteinasesmentioning

confidence: 99%

Proteinase‐Catalyzed Synthesis of Peptide Bonds

Fruton

1982

Advances in Enzymology - And Related Areas of Molecular Biology

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Hypothalamic cathepsin D: Assay and isoenzyme composition

Akopyan

Barchudaryan

Karabashyan

et al. 1979

J of Neuroscience Research

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A sensitive and convenient method of endopeptidase assay using as substrate globin modified with pyridoxal-5-phosphate was used for determination of acid proteinases in bovine hypothalamus separated by isoelectric focusing. The soluble protein fraction of hypothalamus upon elution from Sephadex gave five peaks of proteinase activity at pH 3.2. The properties indicate that these peaks of endopeptidase activity are isoenzyme forms of cathepsin D.

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