Abstract: A novel method of protecting blood coagulation factor IX from proteases during purification or storage is disclosed. High concentrations of one or more water soluble organic or inorganic salts are used to stabilize factor IX, contained within blood plasma-derived solutions, or contained within solutions derived from other sources, against conversion to clinically unacceptable peptide structures such as factor IXa, and/or degraded factor IX peptides. The technique is useful in stabilizing intermediate purity factor IX preparations during purification, and in maintaining the integrity of purified factor IX during long term storage. Stable high specific activity factor IX preparations are also disclosed.

Abstract: A novel method of protecting blood coagulation factor IX from proteases during purification or storage is disclosed. High concentrations of one or more water soluble organic or inorganic salts are used to stabilize factor IX, contained within blood plasma-derived solutions, or contained within solutions derived from other sources, against conversion to clinically unacceptable peptide structures such as factor IX.sub.a, and/or degraded factor IX peptides.The technique is useful in stabilizing intermediate purity factor IX preparations during purification, and in maintaining the integrity of purified factor IX during long term storage. Stable high specific activity factor IX preparations are also disclosed.

Abstract: New peptides are disclosed which have biological activity of the same type as known calcitonins and which do not have a disulfide bond connecting the cysteines at positions one and seven. Also resin peptides are disclosed which may be converted to peptides having such biological activity; and processes for producing said resin peptides and said calcitonin partially protected peptides.

Abstract: Peptides having adrenocorticotropic hormone activity and resin peptides useful in preparation of such peptides, particularly such peptides having asparagine at the carboxyl end thereof and more particularly such peptides having from 19 to 25 amino acids in their amino acid chains. The invention further involves new processes for the preparation of such peptides.

Abstract: Peptide amides having biological activity and resin peptide amides useful in the preparation of peptides having biological activity, particularly such peptides containing the structure ##STR1## in which R is divinylbenzene crosslinked polystyrene and Bz is benzyl, p-methoxybenzyl, p-chlorobenzyl, p-nitrobenzyl, or benzhydryl, and in which phe and glu are residues of the amino acids phenylalanine and glutamic acid; and processes for preparing such peptide amides.Resin peptide amides are disclosed which contain amino acid chains identical with the amino acid chains of natural peptides having biological activity. Other resin peptide amides are disclosed which contain amino acid chains in which the amino acid residues differ in kind or sequence from amino acid chains of natural biologically active peptides but from which peptides having biological activity may be derived.

Abstract: Pharmaceutical preparations and methods of using the same to treat a host having a condition requiring vasoconstrictive therapy. The preparations comprise a pharmaceutically acceptable carrier and a guanidine compound, or non-toxic acid addition salt thereof, having the structural notation: ##SPC1##Wherein: R.sub.1 is hydrogen or alkyl having 1-4 carbon atoms; R.sub.2 is hydrogen, hydroxy, chloro, fluoro or bromo; and R.sub.3 is hydrogen or the same as R.sub.2 when R.sub.2 is chloro, bromo or fluoro.