External key makro for processing Atari Lynx’s external keyboard Key events are handled with a callback function. It is possible to redefine key macros by the user (for example for playing music). This callback function is called with two parameters. The first one is a pointer to a key macro table. This table is the address of a global table that contains the definition of all key macros that are used.
SYNTAX The syntax of the callback function is the following: callback(void **key_table,int key_table_size)
key_table is a pointer to the key macro table.
key_table_size is the size of the table. This is defined in the external variables/keymacro/external.h file.
The callback function must return 0 if the callback doesn’t have to handle the key event.
If the callback has to handle the key event, it must return 1 if the user callback can handle the event and 2 if the real callback can handle the event.
Note: a lot of the tables (like the table for the buttons) are not supported by the callback function.
typedef void callback(void **key_table, int key_table_size);
extern callback *keymacro_register;
int keymacro_is_valid(int key);
void keymacro_keystroke(int key);
int main(int argc, char **argv) {
callback *key_table;
int key_table_size;
if (keymacro_register!= NULL) {
return 0;
if (!keymacro_register_init()) {
return 1;
key_table = keymacro_register_get_key_table();
if (key_table!= NULL) {
key_table_size = keymacro_register_get_key_table_size();
printf(“keymacro_register_get_key_table() returns %d, key_table_size=%d
“,key_table, key_table_size);
if (key_table_size!= sizeof(k_table)) {
printf(“Can’t get the key macro table
return 2;
return 0;
keymacro_register_init 384a16bd22

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Inhibition of protein kinase C (PKC) in liver plasma membrane vesicles with the phorbol ester phorbol 12,13-dibutyrate (PDBu) decreased the rate of Ca2+-ATPase inhibition caused by 5-hydroxytryptamine (5-HT) and angiotensin II. This suggests that PKC is necessary for the full activation of liver plasma membrane Ca2+-ATPase by 5-HT and angiotensin II. However, PDBu did not affect the maximal rate of Ca2+-ATPase inhibition caused by 5-HT and angiotensin II. These results are similar to those for the effects of the phosphatidylcholine-specific phospholipase C, suggesting that PKC is not involved in the Ca2+-ATPase regulation by 5-HT and angiotensin II through phosphatidylcholine hydrolysis. The PKC inhibitor Ro 31-75


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