Report of Committee A, 1959-1960

Fellman, David

doi:10.2307/40215020

AAUP Bulletin

1960

DOI: 10.2307/40215020

|View full text |Cite

Report of Committee A, 1959-1960

David Fellman¹

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1964

1972

Publication Types

Select...

Article2

Relationship

Self Cite0

Independent2

Authors

Journals

Cited by 2 publications

(1 citation statement)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For a number of reasons, they considered that the two activities represented distinct enzymes. However, as analytical procedures improved; reports from many laboratories made it appear more likely that a single enzyme acts on both substrates (5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16). In view of their evidence that a partially purified enzyme from guinea pig kidney decarboxylated a large number of aromatic -amino acids, including DOPA and 5-hydroxytryptophan, Lovenberg, Weissbach, and Udenfriend (i4) proposed that the enzyme be named "aromatic i-amino acid decarboxylase".…”

mentioning

confidence: 99%

On the Identity of DOPA Decarboxylase and 5-Hydroxytryptophan Decarboxylase

Christenson

Dairman

Udenfriend

1972

Proc. Natl. Acad. Sci. U.S.A.

199

View full text Add to dashboard Cite

Simultaneous immunological titration of DOPA and 5-hydroxytryptophan decarboxylase activities, from a number of tissues of various species, showed that the two activities were not distinguishable with a monospecific antiserum to hog kidney decarboxylase. Together with previous findings, these data firmly establish thb concept that in mammalian tissues the two enzyme activities are associated with a single protein, namely aromatic L-amino acid decarboxylase.The enzymatic synthesis of the biogenic amines serotonin, dopamine, and norepinephrine involves decarboxylation of the corresponding amino acids, 5-hydroxytryptophan and 3.4-dihydroxyphenylalanine (DOPA). DOPA decarboxylase (EC 4.1.1.26) was the first enzyme of the catecholamine biosynthetic pathway to be discovered (1). After the isolation and identification of serotonin (2, 3), Clark, Weissbach, and Udenfriend (4) found significant DOPA decarboxylase activity in their most highly purified preparations of 5-hydroxytryptophan decarboxylase (EC 4.1.1.28) from guinea pig kidney. For a number of reasons, they considered that the two activities represented distinct enzymes. However, as analytical procedures improved; reports from many laboratories made it appear more likely that a single enzyme acts on both substrates (5-16). In view of their evidence that a partially purified enzyme from guinea pig kidney decarboxylated a large number of aromatic -amino acids, including DOPA and 5-hydroxytryptophan, Lovenberg, Weissbach, and Udenfriend (i4) proposed that the enzyme be named "aromatic i-amino acid decarboxylase".Because the amiies resulting from decarboxylation are localized differently and are thought to have distinct physiological functions, many investigators have found it difficult to accept the hypothesis that the same enzyme is involved in both pathways. The recent demonstration that a single, homogeneous enzyme from hog kidney decarboxylates all the naturally occurring aromatic amino acids (17) is a necessary, but not a sufficient, condition for the "single enzyme" hypothesis. The possibility remains that a second enzyme may also exist, at least in some tissues. Recently, Sims and Bloom (18) have reported that, after intracisternal administration of 6-hydroxydopamine to rats, DOPA decarboxylase activities were substantially decreased in certain areas of the brain, while the 5-hydroxytryptophan decarboxylase activities were no different from controls.In the present report, evidence is presented in support of the "single enzyme" hypothesis. It is shown that DOPA decarboxylase and 5-hydroxytryptophan decarboxylase activities are not immunologically distinguishable. DOPA decarboxylase activity was assayed as described (17). The availability of carboxyl-labeled 5-hydroxytryptophan made it possible to assay 5-hydroxytryptophan decarboxylase by a basically similar method. All conditions were the same as those for the DOPA decarboxylase assay, with the following exceptions: the buffer was Tris * HCl (pH 8.

show abstract

mentioning

confidence: 99%

On the Identity of DOPA Decarboxylase and 5-Hydroxytryptophan Decarboxylase

Christenson

Dairman

Udenfriend

1972

Proc. Natl. Acad. Sci. U.S.A.

199

View full text Add to dashboard Cite

show abstract

Overall survey of transmission-performance planning

Williams¹

1964

Proc. Inst. Electr. Eng. UK

View full text Add to dashboard Cite

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Report of Committee A, 1959-1960

Cited by 2 publications

References 0 publications

On the Identity of DOPA Decarboxylase and 5-Hydroxytryptophan Decarboxylase

On the Identity of DOPA Decarboxylase and 5-Hydroxytryptophan Decarboxylase

Overall survey of transmission-performance planning

Contact Info

Product

Resources

About