O. Frohlich et Lg. Young, MOLECULAR-CLONING AND CHARACTERIZATION OF EPI-1, THE MAJOR PROTEIN INCHIMPANZEE (PAN-TROGLODYTES) CAUDA EPIDIDYMAL FLUID, Biology of reproduction, 54(4), 1996, pp. 857-864
A 27-kDa glycoprotein comprises approximately 20% of the total protein
in chimpanzee (Pan troglodytes) cauda epididymal fluid. Polyclonal an
tibodies generated against this glycoprotein react with 27- and 25-kDa
components in chimpanzee cauda epididymal fluid and in human, gorilla
, chimpanzee, and monkey seminal fluid. According to microsequencing,
the 27- and 25-kDa components (chimpanzee EPI-1) are identical to the
cloned putative human epididymal protein HE1. Screening of a chimpanze
e epididymal cDNA library enabled isolation of a cDNA clone of chimpan
zee EPI-1. On the cDNA level, chimpanzee EPI-1 and hu man HE1 are 99%
identical. Northern analysis localized chimpanzee EPI-1 mRNA to the di
stal caput epididymidis. With EPI-1 primers, polymerase chain reaction
of reverse-transcribed rhesus monkey (Macaca mulatta) epididymal RNA
enabled isolation of a rhesus monkey EPI-1 cDNA clone. The derived ami
no acid sequence of rhesus monkey EPI-1 is identical to chimpanzee EPI
-1 and to human HE1. Northern analysis localized rhesus monkey EPI-1 m
RNA to the distal caput and the proximal corpus epididymidis. Northern
analysis also showed that chimpanzee EPI-1 and rhesus monkey EPI-1 ge
ne products are expressed specifically in the epididymis and not in an
y other tissue examined.