Tissue specific variation in the isozyme pattern of the ap( 1) Acid phosphatase in maize.

M A N Y examples of multiple forms of enzymes are now known (WR~BLEWSKI 1961; KAPLAN 1963; LATNER and SKILLEN 1968). These multiple forms were designated isozymes by MARKERT and MBLLER (1959). Some multiple forms are controlled by alleles of a given gene (ALLEN 1961; ALLEN, MISCH and MORRISON 1963; LEVINTHAL, SINGER and FETHEROLF 1962). Others result from the independent action of more than one gene in some instances with the formation of hybrid enzyme between the products of the two genes as in lactate dehydrogenase (APPELLA and MARKERT 1961; CAHN, KAPLAN, LEVINE and ZWILLING 1962) and in other instances without hybrid enzyme formation (SCHWARTZ 1964a; BECKMAN, SCANDALIOS and BREWBAKER 1964). Tissue specific variation in an enzyme controlled by a single allele of the E, esterase in maize was described by SCHWARTZ (1964b) and ENDO and SCHWARTZ (1966). The NN pH 7.5 esterase synthesized under the control of the ElN allele in the seedlings and endosperm showed identical electrophoretic migration rates in starch gel. However, they differed in their inactivation by urea. Electrophoretic studies of acid phosphatase isozymes in a number of organisms were reviewed by LATNER and SKILLEN (1968) and in maize by BROWN and ALLARD (1969). This paper describes the AP, acid phosphatase isozymes in maize. Results will be reported to show the presence of different forms of AP, acid phosphatase in the scutellum and the pollen, while both are present in the leaf. In identical genotypes, the single AP, isozyme in pollen migrates somewhat faster than the single AP, isozyme in the scutellum.