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B. BOETTCHER

Summary.

ABO blood group antigens on spermatozoa have been investigated using the agglutination inhibition technique. Antigens were not detected on spermatozoa from non-secretors, though they were detected on spermatozoa from secretors. Further, it has been demonstrated that spermatozoa will adsorb ABO antigens from aqueous solutions. The inhibition titres of seminal plasma and of spermatozoa from secretors were shown to be correlated.

It is concluded that ABO antigens are found only on seminal spermatozoa from secretors and that these are adsorbed from the seminal plasma.

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B. BOETTCHER

Summary.

Washed spermatozoa from an O non-secretor have been incubated with seminal plasma from an A secretor and have been shown then to have developed the capacity of inhibiting anti-H and anti-A test solutions. This demonstration is in agreement with the findings of Edwards, Ferguson & Coombs (1964) who, in contrast to earlier workers, were unable to detect ABO blood group antigens on spermatozoa from non-secretors, though they were able to detect them on spermatozoa from secretor donors.

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B. A. BALDO and B. BOETTCHER

Summary.

Using a haemagglutination technique, heterologous antisera to both the seminal plasma and spermatozoa of man, possum, rabbit and ram and the whole homogenized epididymis and vas deferens of the rat, were found to show immunological cross-reaction with homologous erythrocytes. Cross-reaction between rabbit antiserum to rooster seminal plasma and chicken erythrocytes was observed, but cross-reaction was not seen with antiserum to rooster spermatozoa.

Rabbit antiserum to bull seminal plasma haemolysed bovine erythrocytes, but haemolysis was not observed with antiserum to bull spermatozoa.

The results obtained are discussed with particular reference to other papers reporting such cross-reacting antigens.

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T. K. ROBERTS and B. BOETTCHER

Summary.

SCA has been identified as an iron-binding protein present in seminal plasma. It has an electrophoretic mobility similar to transferrin, and different from lactoferrin, whereas it shares immunological characteristics with lactoferrin not possessed by transferrin. The name scaferrin is proposed for this compound.

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B. BOETTCHER and D. J. KAY

While studying spermagglutinating sera, a number of sera which were positive in a microagglutination test (Franklin & Dukes, 1964), but which were negative in a macroscopic test in gelatin medium (Kibrick, Belding & Merrill, 1952) were found (Boettcher, Kay, Rümke & Wright, 1971). It appears that the agglutinins in these sera are not immunoglobulins (Boettcher & Kay, 1969; Boettcher, Hay, Kay, Baldo & Roberts, 1970). During procedures for fractionating these sera, much of the activity is often lost. One cause of the loss is dialysis. Sera, dialysed overnight against phosphate-buffered saline, have shown marked decreases in their spermagglutinating activities, though their haemagglutinating activities have been unaltered (Boettcher & Kay, 1969; Boettcher et al., 1970).

Reported here are the results of experiments designed to determine whether the

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R. V. Hyne, R. N. Murdoch and B. Boettcher

Summary. The metabolism and motility of human ejaculated spermatozoa incubated in vitro with steroids were studied. Progesterone and norethynodrel depressed the respiration, glycolytic metabolism and the motility of washed spermatozoa. Lynoestrenol did not affect the respiration or glycolysis of the spermatozoa, but did inhibit motility. Oestradiol did not cause any consistent alteration of the sperm metabolism, and did not affect the motility. Progesterone and norethynodrel appear to act on the plasma membrane of human spermatozoa to increase its permeability and hence to facilitate the loss of essential cofactors required for the glycolytic and oxidative processes.