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F M BUMPUS

Publications and source records attributed to F M BUMPUS.

At least 19 recordsLinked to original sources
PubMed1963

Angiotensinase with a high degree of specificity in plasma and red cells.

A peptidase with a high degree of specificity for angiotensin II occurs in normal human plasma and red cells. Preparations from both sources have the same pH optimum, require calcium ions, and hydrolyze valyl(5)- or isoleucyl(5)-angiotensin II, but do not hydrolyze beta-aspartyl(1)-angiotensin II, arginyl(1)-angiotensin II or deaminoangiotensin II. This enzyme, given the name angiotensinase A, requires alpha-L-aspartic acid or alpha-L-asparagine as the N-terminal amino acid in its angiotensin substrate, and thus differs from kidney leucine aminopeptidase. Other peptidases known to hydrolyze angiotensin also hydrolyze at least one of the other angiotensin analogs with substitution in the one position.

Angiotensin II↗
PubMed1962

Angiotensin II: its metabolic fate.

Randomly labeled tritiated angiotensin has been prepared with a specific activity of 300 microc/mg and with undiminished pressor and oxytocic activity. After infusion, angiotensin accumulated in the kidneys, adrenal glands, and uterus. Thirty minutes after infusion high levels of radioactivity appeared in brain, but the electrophoretic mobility differed from that of angiotensin II. Incubation of angiotensin with hemolyzed human red blood cells or diluted human plasma rapidly inactivated the pressor activity with production of metabolic products separable by paper chromatography. But if undiluted plasma is used with incubation up to 6 hours, no loss of activity occurs.

Adrenal Glands↗
PubMed1961

Angiotensin.

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Angiotensin Amide↗
PubMed1959

Angiotensin.

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Angiotensins↗