A bispecific, bivalent antibody comprising a first antigen-binding site that specifically binds to human VEGF and a second antigen-binding site that specifically binds to human ANG-2, characterized in that said antibody comprises i) the heavy chain and the light chain of a first full length antibody that specifically binds VEGF with said first antigen-binding site comprising as heavy chain variable domain the SEQ ID NO: 1, and as light chain variable domain the SEQ ID NO: 2; and ii) the modified heavy chain and modified light chain of a second full length antibody that specifically binds ANG-2, wherein the constant domains CL and CH1 are replaced by each other, with said second antigen-binding site comprising as heavy chain variable domain the SEQ ID NO: 3, and as light chain variable domain the SEQ ID NO: 4, and wherein the bispecific, bivalent antibody has a constant region of human IgG1 subclass, and wherein the antibody is characterized in that the CH3 domain of the heavy chain of the first full length antibody of i) and the CH3 domain of the heavy chain of the second full length antibody of ii) each meet at an interface which comprises an alteration in the original interface between the antibody CH3 domains; wherein a) in the CH3 domain of one heavy chain an amino acid residue is replaced with an amino acid residue having a larger side chain volume, thereby generating a protuberance within the interface of the CH3 domain of one heavy chain which is positionable in a cavity within the interface of the CH3 domain of the other heavy chain, and wherein the CH3 domain of the one heavy chain comprises a T366W mutation, numbering according to EU index of Kabat; and wherein b) in the CH3 domain of the other heavy chain an amino acid residue is replaced with an amino acid residue having a smaller side chain volume, thereby generating a cavity within the interface of the second CH3 domain within which a protuberance within the interface of the first CH3 domain is positionable, and wherein the CH3 domain of the other heavy chain comprises T366S, L368A, and Y407V mutations, numbering according to EU index of Kabat; and and wherein c) the antibody comprises an additional Y349C mutation in one CH3 domain and an additional S354C mutation in the other CH3 domain (forming a interchain disulfide bridge), numbering according to EU index of Kabat. i) the heavy chain and the light chain of a first full length antibody that specifically binds VEGF with said first antigen-binding site comprising as heavy chain variable domain the SEQ ID NO: 1, and as light chain variable domain the SEQ ID NO: 2; and ii) the modified heavy chain and modified light chain of a second full length antibody that specifically binds ANG-2, wherein the constant domains CL and CH1 are replaced by each other, with said second antigen-binding site comprising as heavy chain variable domain the SEQ ID NO: 3, and as light chain variable domain the SEQ ID NO: 4, and a) in the CH3 domain of one heavy chain an amino acid residue is replaced with an amino acid residue having a larger side chain volume, thereby generating a protuberance within the interface of the CH3 domain of one heavy chain which is positionable in a cavity within the interface of the CH3 domain of the other heavy chain, and wherein the CH3 domain of the one heavy chain comprises a T366W mutation, numbering according to EU index of Kabat; and wherein b) in the CH3 domain of the other heavy chain an amino acid residue is replaced with an amino acid residue having a smaller side chain volume, thereby generating a cavity within the interface of the second CH3 domain within which a protuberance within the interface of the first CH3 domain is positionable, and wherein the CH3 domain of the other heavy chain comprises T366S, L368A, and Y407V mutations, numbering according to EU index of Kabat; and and wherein c) the antibody comprises an additional Y349C mutation in one CH3 domain and an additional S354C mutation in the other CH3 domain (forming a interchain disulfide bridge), numbering according to EU index of Kabat.