Ultrastructural localization of acid phosphatase and alkaline phosphatase within oogonia of Achlya recurva

Oogonial development of Achlya recurva Cornu (sensu Latham) was studied utilizing the Barka-Anderson and Hugen Borgers modifications of the Gomori reaction. The differentiation of the oogonium was subdivided into stages A-1, A-2, and A-3. Transmission electron microscopy revealed that acid phosphata...

Full description

Saved in:
Bibliographic Details
Published in:Mycologia 1984, Vol.76 (1), p.85-98
Main Authors: Aliaga, G.R, Ellzey, J.T
Format: Article
Language:English
Subjects:
Achlya recurva
acid phosphatase
alkaline phosphatase
Cytoplasmic vesicles
Endoplasmic reticulum
Enzymes
fungi
Lipids
Oogonia
Oospores
Phosphatases
Reaction products
Sodium
ultrahistochemistry
ultrastructure
Vacuoles
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Oogonial development of Achlya recurva Cornu (sensu Latham) was studied utilizing the Barka-Anderson and Hugen Borgers modifications of the Gomori reaction. The differentiation of the oogonium was subdivided into stages A-1, A-2, and A-3. Transmission electron microscopy revealed that acid phosphatase reaction product (ACP) was localized primarily within apical vesicles of oogonial protuberances within stage A-1 oogonia. Other sites of ACP within A-1 oogonia included vesicles beneath the oogonial wall and the periphery of the oogonial wall. Numerous vesicles within antheridia and areas of vacuolation such as the oogonial stalk had substantial amounts of ACP. Within the A-2 oogonia, ACP was localized primarily at the periphery of the oogonial wall. In contrast, in the A-3 oogonia ACP was very prevalent within dictyosomes and the granular component of "fingerprint" vacuoles. Alkaline phosphatase reaction product (ALP) was observed in dictyosomes, cytoplasmic vesicles, oogonial walls, "fingerprint" vacuoles, and nuclei of A-3 oogonia as well as extra-cellularly. Possible functions of these enzymes in relationship to sex-organ morphogenesis are discussed.
ISSN:0027-5514
1557-2536
DOI:10.1080/00275514.1984.12023812