Recombinant plasmids containing human and baboon cDNA have been screened for a,-antitryJsin, a major serine protease inhibitor present in blood. One plasmid, designated pBaoda2, was found to contain a cDNA insert of 1352 base pairs coding for the baboon inhibitor. It included 45 nucleotides that code for 15 amino acids present in the amino-terminal signal sequence of the protein, 1182 nucleotides that code for 394 amino acids in the mature protein, a stop codon, and a noncoding region of 76 nucleotides. Comparison of the amino acid sequences of baboon a1-antitrypsin, human antithrombin III, and chicken ovalbumin indicated that these three proteins are about 30% homologous. A second plasmid, designated pHalal, was found to contain a human cDNA insert of 306 base pairs. This plasmid coded for 69 amino acids present in the carboxyl-terminal region ofhuman al-antitrypsin. The human and baboon cDNAs and their amino acid sequences are >96% homologous.a1-Antitrypsin [a1-proteinase inhibitor (1)] is an important protease inhibitor present in mammalian blood. Its major physiological function appears to be the inhibition ofneutrophil elastase, a potent protease that hydrolyzes structural proteins (2). It also inhibits many other serine proteases, however, including trypsin, chymotrypsin, collagenase, thrombin, kallikrein, and plasmin (2). The inhibition of the various proteolytic enzymes is due to the formation of a stable, inactive complex containing 1 mol of enzyme and 1 mol of inhibitor. a1-Antitrypsin is a glycoprotein synthesized in the liver. It is composed of a single polypeptide chain (Mr, 50,000) (3) and three carbohydrate chains (4). At present, about 40% of the amino acid sequence has been reported (5-7). This includes regions from the aminoterminal and carboxyl-terminal portions of the molecule.A low level of a1-antitrypsin in the blood is often associated with chronic obstructive pulmonary emphysema and infantile liver cirrhosis (2,8). At present, more than 30 different genetic variants have been identified (1, 9). Several of these are associated with low concentrations of the inhibitor in the blood.The normal plasma level of ar-antitrypsin is about 2 mg/ml. Under most inflammatory conditions, an acute-phase response is initiated and the concentration of a1-antitrypsin is substantially increased (2, 10). In order to study a1-antitrypsin deficiency at the molecular level and examine the mechanism ofthe acute phase response, we have constructed a1-antitrypsin cDNA clones from human and baboon liver mRNAs. In this communication, we report the sequence for a partial human cDNA and a nearly full-length baboon cDNA for a1-antitrypsin and compare the amino acid sequence of this protein with that of antithrombin III and ovalbumin.

Level II, prospective case series.

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The authors report on 142 patients treated surgically for chronic pancreatitis. They had an average age of 43.5; 34.5% were calcific; 62.7% were alcoholics: 28.9% had cysts; 19% had diabetes; 16.9% had steatorrhea; and all had pain. A follow-up of 55 patients undergoing pancreaticojejunostomy showed that, 4--21 years following operation 16 had marked improvement, 11 had some relief, four were not relieved from pain, and 24 had died, three within one month postoperatively and 21 later. Eighty to ninety-five per cent pancreatectomy was more effective in relieving pain in the 9 patients subjected to this type of resection than was the 50--80% pancreatic resection used in 16 patients. Pancreaticoduodenectomy was of some value in three of five patients so operated. Celiac ganglionectomy, used in 22 patients, and sphincteroplasty, used in 35 patients, were less effective in relieving symptoms than the other procedures.

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